Protein surface recognition by synthetic receptors: A route to novel submicromolar inhibitors for α-chymotrypsin

Hyung Soon Park, Qing Lin, Andrew D. Hamilton

Research output: Contribution to journalArticlepeer-review

Abstract

A family of synthetic receptors for protein surface recognition has been prepared. The receptors are based on a design in which four peptide loops are arrayed around a central calilx[4]arene core. By varying the sequence of the loop regions a range of differently functionalized receptor surfaces approximately 450 Å2 in area can be prepared. From this family we have identified potent inhibitors of chymotrypsin that function by binding to the surface of the protein. The most potent of these (1) shows slow binding kinetics in an analogous manner to several of the natural protein proteinase inhibitors. Detailed kinetic analysis showed 1 to be a competitive inhibitor with K(i) and K(i)* values of 0.81 and 0.11 μM, respectively.

Original languageEnglish (US)
Pages (from-to)8-13
Number of pages6
JournalJournal of the American Chemical Society
Volume121
Issue number1
DOIs
StatePublished - Jan 13 1999

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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