Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics

N R Graciani; K Y Tsang; S L McCutchen; J W Kelly

doi:10.1016/s0968-0896(00)82048-9

Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics

Bioorg Med Chem. 1994 Sep;2(9):999-1006. doi: 10.1016/s0968-0896(00)82048-9.

Authors

N R Graciani¹, K Y Tsang, S L McCutchen, J W Kelly

Affiliation

¹ Department of Chemistry, Texas A&M University, College Station 77843-3255.

PMID: 7712134
DOI: 10.1016/s0968-0896(00)82048-9

Abstract

Acyclic beta-sheet structure can be nucleated in heptapeptides when the 4-(2-aminoethyl)-6-dibenzofuranpropanoic acid residue (1) is flanked in sequence by two His residues, a His residue and a hydrophobic residue or by two hydrophobic residues. Acyclic beta-sheet peptidomimetics having an appropriate sequence have sufficient structural integrity to exhibit antimicrobial activity equivalent to that of gramicidin S.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Amino Acids / chemistry*
Chemical Phenomena
Chemistry, Physical
Circular Dichroism
Histidine / chemistry*
Kinetics
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Oligopeptides / chemical synthesis
Oligopeptides / chemistry*
Oligopeptides / pharmacology*
Peptides / agonists*
Peptides, Cyclic / chemical synthesis
Peptides, Cyclic / chemistry
Peptides, Cyclic / pharmacology
Protein Conformation
Protein Structure, Secondary*
Structure-Activity Relationship

Substances

Amino Acids
Oligopeptides
Peptides
Peptides, Cyclic
Histidine