Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides |
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Authors: | Pal-Bhowmick Ipsita Pandey Ramendra Pati Jarori Gotam K Kar Santosh Sahal Dinkar |
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Affiliation: | a Tata Institute of Fundamental Research, Colaba, Mumbai 400005, India b School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India c International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Road, New Delhi 110067, India |
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Abstract: | Ribonuclease S peptide and S protein offer a unique complementation system to understand the finer features of molecular recognition. In the present study the S peptide (1-16), and its retro and retro-inverso analogs have been analyzed for their structural and biological attributes. RPHPLC, CD, and NMR analyses have revealed that the physicochemical and conformational properties of the S peptide are distinct from those of its retro and retro-inverso analogs. On the functional side, while the S peptide complemented the S protein to give RNase activity, was recognized by anti-S peptide antibodies and induced T cell proliferation, neither the retro nor the retro-inverso S peptides could do so. |
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Keywords: | APC, antigen presenting cell CD, circular dichroism CFA, complete Freund&rsquo s adjuvant ELISA, enzyme-linked immunosorbent assay NMR, nuclear magnetic resonance NOE, nuclear Overhauser effect poly-C, poly-cytidine R, retro RI, retro-inverso RIS peptide, retro-inverso S peptide RP, retro-peptide RS peptide, retro S peptide RPHPLC, reverse phase high performance liquid chromatography TFE, trifluoroethanol |
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