Structure-guided design of peptidic ligand for human prostate specific antigen

Hassan, MD. Imtaiyaz ; Kumar, Vijay ; Somvanshi, Rishi K. ; Dey, Sharmistha ; Singh, Tej P. ; Yadav, Savita (2007) Structure-guided design of peptidic ligand for human prostate specific antigen Journal of Peptide Science, 13 (12). pp. 849-855. ISSN 1075-2617

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Prostate specific antigen (PSA) is a member of kallikrein family having serine protease-like activity and acts as a prognostic marker of prostate carcinoma. Various studies have been performed on inhibition of PSA and such targeting requires the identification of highly selective peptide inhibitors. PSA was purified from human seminal plasma by rapid and efficient methods, and binding studies for various peptides were carried out by fluorescence spectroscopy and SPR. The 'S' of PSA is predominated by hydrophobic residues, and hence many hydrophobic peptides were used to determine their binding affinity to PSA by fluorescence spectroscopy. We observed that LLFW, FFKW, and KFW binds strongly to PSA, among them LLFW showed strong binding. SPR also showed strong binding affinity of PSA toward peptides with hydrophobic and basic residues. Among the peptides used, FWYS showed dramatic increase in binding affinity (10-10M). The peptides analyzed for binding studies, suggests that peptide with Trp residue along with basic or hydrophobic amino acids may be useful for designing specific inhibitors for PSA. The strong affinities of designed peptides for PSA can be a valuable tool for designing therapeutic agents for prostate carcinomas.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Peptide, Inhibitor; Three-Dimensional Structure; Prostate Carcinoma; Kallikrein; Tumor Proliferation; Chymotrypsin; Structure Based Drug Design
ID Code:49134
Deposited On:18 Jul 2011 14:42
Last Modified:18 Jul 2011 14:42

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