TY - JOUR
T1 - A review of the utility of soluble peptide combinatorial libraries
AU - Pinilla, Clemencia
AU - Appel, Jon
AU - Blondelle, Sylvie
AU - Dooley, Colette
AU - Dörner, Barbara
AU - Eichler, Jutta
AU - Ostresh, John
AU - Houghten, Richard A.
PY - 1995
Y1 - 1995
N2 - This is paper reviews the preparation and use of soluble synthetic combinatorial libraries (SCLs) made up of millions of peptide and nonpeptide sequences for the identification of highly active individual compounds. First presented in 1991. SCLs have been prepared in a number of different lengths and formats, and are composed entirely of L‐, D‐, and unnatural amino acids. Also, existing peptide libraries have been chemically transformed to yield large diversities of nonpeptidic compounds. This review encompasses the published work from this laboratory using SCLs for the identification of antigenic sequences recognized by monoclonal antibodies, novel peptide agonists and antagonists to opioid receptors, new trypsin inhibitors, novel antibacterials, and compounds that inhibit melittin's hemolytic activity. SCLs offer a fundamental, practical advance in the study of interactions between peptide and nonpeptide sequences and their biochemical or pharmacological targets. © 1994 John Wiley & Sons, Inc.
AB - This is paper reviews the preparation and use of soluble synthetic combinatorial libraries (SCLs) made up of millions of peptide and nonpeptide sequences for the identification of highly active individual compounds. First presented in 1991. SCLs have been prepared in a number of different lengths and formats, and are composed entirely of L‐, D‐, and unnatural amino acids. Also, existing peptide libraries have been chemically transformed to yield large diversities of nonpeptidic compounds. This review encompasses the published work from this laboratory using SCLs for the identification of antigenic sequences recognized by monoclonal antibodies, novel peptide agonists and antagonists to opioid receptors, new trypsin inhibitors, novel antibacterials, and compounds that inhibit melittin's hemolytic activity. SCLs offer a fundamental, practical advance in the study of interactions between peptide and nonpeptide sequences and their biochemical or pharmacological targets. © 1994 John Wiley & Sons, Inc.
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U2 - 10.1002/bip.360370306
DO - 10.1002/bip.360370306
M3 - Article
C2 - 7718744
AN - SCOPUS:0028939901
SN - 0006-3525
VL - 37
SP - 221
EP - 240
JO - Biopolymers
JF - Biopolymers
IS - 3
ER -