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Research

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Team

Alumni

K. Santhosh Kumar, PhD

Scientist F

+91-471-2781218

kskumar@rgcb.res.in

santhoshkumar
santhoshkumar

K. Santhosh Kumar, PhD

Scientist F

+91-471-2781218

kskumar@rgcb.res.in

  • Profile

    • PhD in Chemistry (School of Chemical Sciences, Mahatma Gandhi University, Kottayam, Kerala)
    • April 10, 2008 – Present: Scientist EII, RGCB, Thiruvananthapuram
    • April 10, 2004 – April 10 2008: Scientist E1, RGCB, Thiruvananthapuram
    • April 10, 2000 – April 10, 2004: Scientist C, RGCB, Thiruvananthapuram
    • April 10, 2000 – Present: Scientist C, RGCB, Thiruvananthapuram
    • June 02, 2001 – June 05, 2003: Postdoctoral Research Associate, Department of Biochemistry, University of Illinois, Urbana-Champaign, USA
    • Sept 27, 1996 – April 10, 2000: Scientist B, RGCB, Thiruvananthapuram
    • Jan 10, 1996 – Sept 27, 1996: Postdoctoral Research Scientist, RGCB, Thiruvananthapuram
    • Number of students awarded PhD : 3
    • Number of students currently working for PhD : 5
    • Kumar, K. S. & Kumar, G. S. V.A novel, flexible, mechanically stable polymer support for SPPS. US Patent No:10/625894, Awarded in 2007 January, Indian Patent file No: 919/DEL/2003

  • Research

    Synthetic peptides and their derivatives which can act as antibiotics or cell penetrating molecule is of great importance. A fundamental understanding of the influence of their structure, nature of amino acid, sequence on activity and mechanism will be an important part of any future strategy aimed at solving the growing problem of microbial resistance to currently available antibiotics or delivering molecules in specific sites inside the cell without causing cytotoxicity. Our research also involves the design and synthesis of a biodegradable polymer of nano size as drug delivery system and developing new strategy for the chemical synthesis of mini-proteins. Though the foundation of all these areas of research is organic synthesis, chemical biology enables us to tackle these scientific problems on the threshold between chemistry and biology.

    Peptide antibiotics

    The growing problem of resistance against existing antibiotics, coupled with a sustained decline in the success rate of the discovery of new ones, is currently leading to a point in the future where many infections could essentially be untreatable by the compounds that are currently available. Amphibians and insects have enjoyed remarkable evolutionary success and emerged as the most successful clade of all organisms constituting close to 80% of all animal life forms. Living and evolving closely with other dominant life forms such as microbes, they have developed an amazingly strong resistance to infectious microbes and in many cases established symbiotic associations with microbes. Peptides which can kill broad spectrum of microbes are widely distributed throughout the animal and plant kingdoms is the defensive weapon that give them protection and served a fundamental role in the successful evolution of complex multicellular organisms. These molecules could act as the possible candidate molecules against microbial infection.

    Several potential host defense peptides (mini proteins) that inhibit microbial growth in microgram level were isolated and characterised from skin secretion of bicoloured frog Clinotarsus curtipes, endemic to Western Ghats, Kerala. The most potent fraction obtained during purification contains seven peptides of which the first six peptides belongs to brevinin-1 sub-family and the 7th peptide belongs to brevinin-2 sub-family. A peptide B1CTcu4 is very effective against the superbug MRSA and another one B1CTcu5 is highly effective against Mycobacterium tuberculosis. Our studies also showed that different frog species store different classes of peptide. A systematic comparison of frog peptide isolated from the Western Ghats with that known from the temperate climatic region may provide valuable information about the nature of amino acids and their arrangement in a peptide to show antibacterial activity. Mechanism that underlying changes that take place upon AMPs binding with bacterial cell wall can provide valuable information required to design and synthesis novel therapeutic molecules.

    Effect of PEGylation on bio-activity of antimicrobial peptides (AMPs)

    Therapeutic use of AMP as potential antibiotic agents is hampered by their poor in vivo half-life, rapid renal filtration, proteolytic degradation and increased intracellular uptake by the reticuloendothelial system. PEGylation or fatty acid acylation can increase the in vivo stability of a peptide and helps to avoid the immune response. Structure-activity studies using different derivatives can helps to understand the structural requirements of these conjugate to act as an effective anti-infective molecule for therapeutic use. Chemical synthesis of PEGylated AMPs is a challenging problem because the physico-chemical incompatibility of the polymer back bone with the resin bound peptides results lot of steric hindrance during the PEGylation reaction. The reactive site of the hydrophilic bulk PEG molecule may not be available at the polymer bound reactive sites for reaction. A core-shell polymer 3, 3' PEG Bis (1-(4-vinylphenoxy) propan-2-ol) crosslinked polystyrene support in which the reactive functional groups are confined to resin surface was used for the synthesis of PEGylated peptides. Antibacterial potency of a peptide is not seriously affected by its conjugation with mPEG1100.PEGylation did not affect the initial electrostatic interaction between the peptide and the lipid membrane surface but its antibacterial potency decreases which depend upon the molecular weight of PEG. This masking effect provided by the flexible poly ethylene oxide chain will prevents the peptides from aggregation and reduces its hydrophobic nature and hemolytic potential. PEGylation can alter the supramolecular assembly of the conjugate and contribute positively to improve therapeutic indices of AMPs and provide selectivity to bind microbial and mammalian membranes.

    Cell penetrating peptides

    Cell Penetrating Peptides (CPP) has the ability to penetrate into the cell membrane and translocate across it without causing toxicity to the cell. This class of peptides can be used as a delivery system for the transportation drugs, proteins, nucleic acids and other cargos across the cell membrane. Arginine rich peptides having the template R6X6 were synthesised to study the influence of the nature of amino acids and their arrangement in the primary sequence on cell penetrating or antibacterial activity. R6G6 peptideshowed least cell penetrating power compared to other arginine-A/V/M/P peptides and its poor cell penetrating ability is due to the conformational changes resulted from the spacing of arginine with glycine in the peptide chain. The side chains of Glycine, alanine, proline and threonine in arginine rich R6X6 is not enough to provide the required hydrophobic face that can induce bacterial lysis to a peptide. Therefore these peptides are not antibacterial in nature. A minimum of three carbon side chain (like leucine) in arginine rich R6X6 can provide the required hydrophobic face to the peptide and help it to interact effectively with the microbial membrane. In R6V6 the conformational restrictions imparted by valine side chain force the peptide to adopt a beta sheeted conformation which provides a preferential selectivity to the peptide towards the microbial and mammalian membranes. Alpha helical structure and an optimum hydrophobic-hydrophilic character resulted from the amino acid arrangement helped R6A6 to penetrate into the cell nucleus without causing cytotoxicity while in R6V6 the aggregation tendency resulted from the beta sheet arrangement confined its distribution only to cytoplasm.

    Polymer Support for the Chemical Synthesis of Proteins and their analogs by Native Chemical Ligation

    Joining of two peptide fragments by chemoselective reaction between two peptide segments in water at pH 7 to form mini-protein and/or their analogs is still a challenging problem to peptide chemist. A peptide thioester can undergo trans-thio-esterification with N-terminal cysteine residue of another peptide in presence of mercapten. The side chain thiol group of the cysteine residue forms an intermediate with the thioester which spontaneously rearranges to form a five-member ring. The intramolecular nucleophilic attack by the cysteine R-amino group results the formation amide bond at the ligation site. Modified mini-proteins with D-amino acids, N-methyl amino acids, Β-amino acids etc. can be synthesized by this technique which otherwise is not possible by the recDNA technology.

    The main problem associated with the thioester synthesis is its low percentage cleavage from the support and the loss due to Fmoc deprotection with piperidine. Polymer support used for the thioester synthesis can influences the final yield. Every attempt to improve the yield by modifying the standard protocol was failed to produce any improvement. But its synthesis on PS-PEGDA support containing 3-carboxypropane sulfonamide linker enhanced the cleavage yield. The synergistic effect of the polyoxyethylene group in the polymer might help to enhance the activation of iodoacetonitrile which resulted higher cleavage yield. A double linker strategy by introducing a spacer arm rink amide linker between resin and 3-carboxy propane sulfonamide helped to improve the stability of the thioester and the cleavage yield of peptide-α-thioester.

    Target Specific Novel Nano Drug Delivery Systems

    Delivery of high dose of traditional chemotherapeutic agents to tumour sites without causing systemic damage and side effects is still a formidable task. Improved therapeutic index with enhanced specificity, potency and prolonged delivery of the drug is a major impetus for innovation in many therapeutic areas such as cancer, inflammatory and infective disease. A biodegradable polymer that can carry the drug and the target specific moiety can be used as the carrier to deliver the drug at the site of its action is the best choice.

    The nano carrier was developed by synthesising the monomer ethyl (2-acetoxymethyl) acrylate by the microwave assisted MBH reaction between ethyl acrylate and formaldehyde inPEG-200. The monomer was attached to PS-bis(VPP)PEG core-shell polymer support and the carrier synthesis is continued upto the 4th generation. The hydroxyl groups present in the dendrimer was masked with O benzyl protection and the dendrimer synthesis was continued upto 7th generation. Anticancer drug doxorubicin conjugated tetrapeptide Gly-Phe-Leu-Gly was attached to residual hydroxyl groups coupled with succinic acid. The drug can selectively cleaved by the lysosomal enzyme Cathepsin B in a concentration depended manner. The dendrimer synthesis was continued for one more generation to incorporate the target specific molecules

    Peptide ligands with VEGFR-3 binding capabilities were screened using phage display peptide library. Two nine-mer peptides VRL2 and VRL3 with the motif CWEXXHXSC (X any amino acid) was selected as the targeting moiety. Another set of peptide ligands with EGF-R binding capability were designed by computer aided design approach. Many peptides were analysed from the virtual peptide library of putative EGF-R binding peptides by screening them against EGF-receptor structure in silico. EGF-R binding pocket targeted for CAD ligand design was selected with the aid of the PSCAN program. These peptides conjugated with liposome, has the ability to binds the cells by endocytosis, specifically and efficiently in vitro to the respective receptors VEGFR-3 or EGF-R high-expressing cancer cells.These peptides were incorporated to peripheral hydroxyl functional sites of the dendrimer. After removing the O benzyl protection an optimum amount of PEG-200 was incorporated to improve the solubility of the carrier in aqueous medium and the whole system was tested for its efficiency.

  • Publications

    1. Parvin Abraham 1, Sanil George 1, K. Santhosh Kumar* Novel antibacterial peptides from the skin secretion of the Indian bicoloured frog Clinotarsus curtipes Biochimie 2014 97, 144-151
    2. Won-Tak Choi, Santhosh Kumar, Navid Madani, Xiaofeng Han, Shaomin Tian, Chang-Zhi Dong, Dongxiang Liu, Srinivas Duggineni, Jian Yuan, Joseph G. Sodroski, Ziwei Huang and Jing An "A Novel Synthetic Bivalent Ligand To Probe Chemokine Receptor CXCR4 Dimerization and Inhibit HIV-1 Entry" Biochemistry. 2012, 51 (36), pp 7078-7086
    3. Dong CZ, Tian S, Choi WT, Kumar S, Liu D, Xu Y, Han X, Huang Z, An J. Critical Role in CXCR4 Signaling and Internalization of the Polypeptide Main Chain in the Amino Terminus of SDF-1a Probed by Novel N-Methylated Synthetically and Modularly Modified Chemokine Analogues. Biochemistry. 2012, 51 (30), pp 5951-5957
    4. Deepu A, Aravind A and Kumar K Engineering chemokines to develop putative anti HIV-1 agents. A Deepu, A Aravind, K Kumar BMC Infectious Diseases. 2012, 12 (Suppl 1), 01
    5. Aravind A, Deepu A, and Kumar K Polyester dendrimers: a versatile nanocarrier for target specific drug delivery, BMC Infectious Diseases 2012, 12 (Suppl 1): 5
    6. Aravind A, Sanil George, and K Santhosh Kumar "Remarkable influence of Microwave heating on Morita Baylis Hillman reaction in PEG-200", Chemistry Central Journal. 2012, 6: 30, 29-31
    7. Dong CZ, Tian S, Madani N, Choi WT, Kumar S, Liu D, Sodroski JG, Huang Z and An J. Role of CXCR4 internalization in the anti-HIV activity of stromal cell-derived factor-1a probed by a novel synthetically and modularly modified-chemokine analog. Exp Biol Med. 2011, 1;236(12):1413-9
  • Team


    Parvin Abraham, PhD Student

    Peptidomic analysis of the skin secreted antibacterial peptides of the frog Clinotarsus curtipes and their structure-function studies

    Cationic host defense peptides (HDPs)/antimicrobial peptides (AMPs) which can destroy broad spectrum pathogens were isolated from the skin secretion of the frog Clinotarsus curtipes, endemic to Western Ghats, Kerala, a biodiversity hot spot in India. They are evolutionarily conserved component of the innate immune response, produced as a part of the host defense mechanism. The most active fraction of the crude skin secretion contain seven peptides having high amino acid sequence homology with Brevinin family AMPs. The first six members are named as brevinin1CTcu1- brevinin1CTcu6 and the 7th member is named as brevinin2CTcu1. These peptides are bactericidal in nature and adopted as alpha helical conformation in bacterial membrane mimetic environment. Except B1CTcu1, these peptides are hemolytic at their respective MICs and are capable of permeabilating into the bacterial outer and inner membrane. Though these peptides can induce cytoplasmic membrane depolarisation, bacterial cell death and membrane depolarisation were found to be two independent events. Any change in amino acid residues in the N-terminal of the peptide will seriously affect the antibacterial potency of the peptide and its removal steadily decreases antibacterial potency. The C-terminal cyclisation though provides a higher hydrophobic character to the peptide, showed no influence on its antibacterial potency but it may have a significant role on initial binding with bacterial membrane.

    parvin
    parvin

    Parvin Abraham, PhD Student

    Peptidomic analysis of the skin secreted antibacterial peptides of the frog Clinotarsus curtipes and their structure-function studies

    Cationic host defense peptides (HDPs)/antimicrobial peptides (AMPs) which can destroy broad spectrum pathogens were isolated from the skin secretion of the frog Clinotarsus curtipes, endemic to Western Ghats, Kerala, a biodiversity hot spot in India. They are evolutionarily conserved component of the innate immune response, produced as a part of the host defense mechanism. The most active fraction of the crude skin secretion contain seven peptides having high amino acid sequence homology with Brevinin family AMPs. The first six members are named as brevinin1CTcu1- brevinin1CTcu6 and the 7th member is named as brevinin2CTcu1. These peptides are bactericidal in nature and adopted as alpha helical conformation in bacterial membrane mimetic environment. Except B1CTcu1, these peptides are hemolytic at their respective MICs and are capable of permeabilating into the bacterial outer and inner membrane. Though these peptides can induce cytoplasmic membrane depolarisation, bacterial cell death and membrane depolarisation were found to be two independent events. Any change in amino acid residues in the N-terminal of the peptide will seriously affect the antibacterial potency of the peptide and its removal steadily decreases antibacterial potency. The C-terminal cyclisation though provides a higher hydrophobic character to the peptide, showed no influence on its antibacterial potency but it may have a significant role on initial binding with bacterial membrane.

    Preethi P. C, PhD Student

    New sulphonamide linker for the polymer supported chemical synthesis of protein by native chemical ligation

    Chemical ligation is the chemoselective reaction of the two peptide segments under neutral medium is an alternative chemical technique for the synthesis of long chain poly peptides, proteins and their analogues. My work involves the development of new polymer support for the synthesis of long chain poly peptides and proteins by chemical ligation technique. Modified mini-proteins with D-amino acids, N-methyl amino acids, Β-amino acids were synthesized by this technique which otherwise is not possible by the recDNA technology. PS-PEGDA support polymer support containing 3-carboxypropane sulfonamide linker enhanced the cleavage yield. The synergistic effect of the polyoxyethylene group in the polymer might help to enhance the activation of iodoacetonitrile which resulted higher cleavage yield. The double linker strategy by introducing a spacer arm rink amide linker between resin and 3-carboxy propane sulfonamide helped to improve the stability of the thioester and the cleavage yield of peptide-α-thioester. Temperature, pH and thiol additives for nucleophilic displacement are other the important factors influencing peptide-a-thioester the cleavage. This technique will be used to synthesize proteins and their analogues.

    preethy
    preethy

    Preethi P. C, PhD Student

    New sulphonamide linker for the polymer supported chemical synthesis of protein by native chemical ligation

    Chemical ligation is the chemoselective reaction of the two peptide segments under neutral medium is an alternative chemical technique for the synthesis of long chain poly peptides, proteins and their analogues. My work involves the development of new polymer support for the synthesis of long chain poly peptides and proteins by chemical ligation technique. Modified mini-proteins with D-amino acids, N-methyl amino acids, Β-amino acids were synthesized by this technique which otherwise is not possible by the recDNA technology. PS-PEGDA support polymer support containing 3-carboxypropane sulfonamide linker enhanced the cleavage yield. The synergistic effect of the polyoxyethylene group in the polymer might help to enhance the activation of iodoacetonitrile which resulted higher cleavage yield. The double linker strategy by introducing a spacer arm rink amide linker between resin and 3-carboxy propane sulfonamide helped to improve the stability of the thioester and the cleavage yield of peptide-a-thioester. Temperature, pH and thiol additives for nucleophilic displacement are other the important factors influencing peptide–a-thioester the cleavage. This technique will be used to synthesize proteins and their analogues.

    Reshmy V, PhD Student

    Isolation, Characterisation and Structure-Function studies of skin secreted peptides from frog Hylarana temporalis

    Host defense peptides (HDPs) are endogenous antibiotics secreted by the endocrine glands, play a multifunctional role in the innate immunity of vertebrates and other organisms. The anuran (frog) skin is one of the most generous sources of antimicrobial peptides. The frog Hylarana temporalis, a member of the Ranidae family, endemic to Western Ghats, India endowed with an excellent chemical defence system consist of peptides against invading microorganisms. Peptides that played multifunctional role in the innate immunity of H. Temporalis were identified and characterised by transcriptomic and peptidomic approaches. After their charecterisation with the help of amino acid and MALDI TOF-TOF based sequencing techniques the peptides were chemically synthesised. Their bio-activity studies showed that they are antibacterial in nature. They adopt helical conformation in membrane mimicking solvents. Several peptide analogues were designed and chemically synthesized to establish mechanism of action and the influence of amino acids, their sequence and conformation on its activity. A thorough analysis of these factors may lead to the development of AMPs as a new class of antibacterial drug with very high therapeutic index.

    reshmy
    reshmy

    Reshmy V, PhD Student

    Isolation, Characterisation and Structure-Function studies of skin secreted peptides from frog Hylarana temporalis

    Host defense peptides (HDPs) are endogenous antibiotics secreted by the endocrine glands, play a multifunctional role in the innate immunity of vertebrates and other organisms. The anuran (frog) skin is one of the most generous sources of antimicrobial peptides. The frog Hylarana temporalis, a member of the Ranidae family, endemic to Western Ghats, India endowed with an excellent chemical defence system consist of peptides against invading microorganisms. Peptides that played multifunctional role in the innate immunity of H. Temporalis were identified and characterised by transcriptomic and peptidomic approaches. After their charecterisation with the help of amino acid and MALDI TOF-TOF based sequencing techniques the peptides were chemically synthesised. Their bio-activity studies showed that they are antibacterial in nature. They adopt helical conformation in membrane mimicking solvents. Several peptide analogues were designed and chemically synthesized to establish mechanism of action and the influence of amino acids, their sequence and conformation on its activity. A thorough analysis of these factors may lead to the development of AMPs as a new class of antibacterial drug with very high therapeutic index.

    Asha R, PhD Student

    Effect of PEGylation and Fatty Acid Acylation on and Membrane Perturbation and Antimicrobial Activity of AMPs

    The efficacy of antibacterial peptides as novel therapeutic agents is hampered by their poor in vivo half-life, rapid renal filtration, proteolytic degradation, and increased intracellular uptake by the reticuloendothelial system. Since these peptides are isolated frogs they can elicit immune response. Repeated administration can result drug neutralisation and rapid clearance by the antibodies. This is partly because of a reduction in activity in the presence of serum plasma. Therapeutic index of AMPs improved by PEGylation or fatty acid acylation and helped to avoid the immune response by preventing the approach of antibodies and reduce loss by renal filtration. It also may help to escape the proteolytic enzymes by creating a molecular 'shield' of PEG or fatty acids around the protein. This conjugation can also help reduces uptake by dendritic cells and interferes with antigen processing thereby greatly reducing or eliminating a foreign proteins immunogenicity. PEGylation is the covalent coupling of non-toxic, hydrophilic PEG to active pharmaceutical ingredients. Hydrophobization of peptides, such as chemical acylation, has been recognized as an efficient method for improving their membrane permeability. Chemical synthesis of PEGylated AMPs is a challenging problem because the physico-chemical incompatibility of the polymer back bone with the resin bound peptides results lot of steric hindrance during the PEGylation reaction. The reactive site of the hydrophilic bulk PEG molecule may not be available at the polymer bound reactive sites for reaction. Therefore a core-shell polymer 3, 3' PEG Bis (1-(4-vinylphenoxy) propan-2-ol) crosslinked polystyrene support in which the reactive functional groups are confined to resin surface was used for the synthesis of PEGylated peptides.

    Asha R
    Asha R

    Asha R, PhD Student

    Effect of PEGylation and Fatty Acid Acylation on and Membrane Perturbation and Antimicrobial Activity of AMPs

    The efficacy of antibacterial peptides as novel therapeutic agents is hampered by their poor in vivo half-life, rapid renal filtration, proteolytic degradation, and increased intracellular uptake by the reticuloendothelial system. Since these peptides are isolated frogs they can elicit immune response. Repeated administration can result drug neutralisation and rapid clearance by the antibodies. This is partly because of a reduction in activity in the presence of serum plasma. Therapeutic index of AMPs improved by PEGylation or fatty acid acylation and helped to avoid the immune response by preventing the approach of antibodies and reduce loss by renal filtration. It also may help to escape the proteolytic enzymes by creating a molecular ‘shield’ of PEG or fatty acids around the protein. This conjugation can also help reduces uptake by dendritic cells and interferes with antigen processing thereby greatly reducing or eliminating a foreign proteins immunogenicity. PEGylation is the covalent coupling of non-toxic, hydrophilic PEG to active pharmaceutical ingredients. Hydrophobization of peptides, such as chemical acylation, has been recognized as an efficient method for improving their membrane permeability. Chemical synthesis of PEGylated AMPs is a challenging problem because the physico-chemical incompatibility of the polymer back bone with the resin bound peptides results lot of steric hindrance during the PEGylation reaction. The reactive site of the hydrophilic bulk PEG molecule may not be available at the polymer bound reactive sites for reaction. Therefore a core-shell polymer 3, 3' PEG Bis (1-(4-vinylphenoxy) propan-2-ol) crosslinked polystyrene support in which the reactive functional groups are confined to resin surface was used for the synthesis of PEGylated peptides.

    Neethu, PhD Student

    Neethu, PhD Student

    Devikanandan C, Junior Research Fellow

    The study involves development of novel polymer nanoparticle based drug releasing system for improving drug administration in cancer chemotherapy. The anticancer property of curcumin and paclitaxel is already well known but the major disadvantage associated with it is their low aqueous solubility. So our study aims to improve the solubility and uptake of the drug by incorporating drug into a biodegradable nanoparticle PLGA which is coated with PEG and then conjugated with folic acid for better uptake. Further characterization and drug release studies of prepared drug loaded nanoparticles are followed by their in-vitro and in-vivo to compare its uptake and efficacy with its free counterparts. The studies are being investigated whether the administration of drug in nano form can enhance the synergistic action of both curcumin and paclitaxel in in vitro and in vivo conditions.

    Devikanandan C
    Devikanandan C

    Devikanandan C, Junior Research Fellow

    The study involves development of novel polymer nanoparticle based drug releasing system for improving drug administration in cancer chemotherapy. The anticancer property of curcumin and paclitaxel is already well known but the major disadvantage associated with it is their low aqueous solubility. So our study aims to improve the solubility and uptake of the drug by incorporating drug into a biodegradable nanoparticle PLGA which is coated with PEG and then conjugated with folic acid for better uptake. Further characterization and drug release studies of prepared drug loaded nanoparticles are followed by their in-vitro and in-vivo to compare its uptake and efficacy with its free counterparts. The studies are being investigated whether the administration of drug in nano form can enhance the synergistic action of both curcumin and paclitaxel in in vitro and in vivo conditions.

    Smitha Devi S, Research assistant

    My job is to help the students and the scientist for their day-to-day activity of the laboratory and the smooth running of various projects. Other responsibilities include chemical synthesis of polypeptides and their derivatives by various techniques, HPLC and flash chromatographic purifications, taking care of various instruments in the laboratory, ordering of fine chemicals for research activity and verifying the stock and sub stock registers in the lab.

    smitha
    smitha

    Smitha Devi S, Research assistant

    My job is to help the students and the scientist for their day-to-day activity of the laboratory and the smooth running of various projects. Other responsibilities include chemical synthesis of polypeptides and their derivatives by various techniques, HPLC and flash chromatographic purifications, taking care of various instruments in the laboratory, ordering of fine chemicals for research activity and verifying the stock and sub stock registers in the lab.

    Aswanikumar S, Technical assistant

    My job is to help the students and the scientist in their various laboratory activities. I am also responsible for maintaining the stock and sub-stock registers in the lab.

    aswani
    aswani

    Aswanikumar S, Technical assistant

    My job is to help the students and the scientist in their various laboratory activities. I am also responsible for maintaining the stock and sub-stock registers in the lab.

  • Alumni