Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-12, Vol.364 (3), p.608-613
Main Authors: Pal-Bhowmick, Ipsita, Pati Pandey, Ramendra, Jarori, Gotam K., Kar, Santosh, Sahal, Dinkar
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
Amino Acid Sequence
ANTIBODIES
ANTIGENS
Binding Sites
CELL PROLIFERATION
CYTIDINE
DICHROISM
ENZYME IMMUNOASSAY
HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY
Mimetics
NITRIC OXIDE
NMR
NUCLEAR MAGNETIC RESONANCE
OVERHAUSER EFFECT
Peptide Fragments - chemistry
Peptide Fragments - immunology
Peptide Fragments - ultrastructure
PEPTIDES
Protein Binding
Retro/retro-inverso peptides
Ribonuclease
Ribonucleases - chemistry
Ribonucleases - immunology
Ribonucleases - ultrastructure
RNA-ASE
S peptide
Structure-Activity Relationship
T cells
T-Lymphocytes - immunology
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.10.056