Modulation of protein-protein interactions by synthetic receptors: Design of molecules that disrupt serine protease-proteinaceous inhibitor interaction

Hyung Soon Park, Qing Lin, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

In the present article we describe the design and evaluation of a synthetic receptor that binds to the exterior surface of chymotrypsin and disrupts its interaction with proteinaceous inhibitors, such as soybean trypsin inhibitor, basic pancreatic trypsin inhibitor, ovomucoid turkey inhibitor, and Bowman-Birk inhibitor. Using enzyme kinetics, nondenaturing gel electrophoresis, and gel filtration chromatography we show that the receptor is particularly effective at blocking the chymotrypsin-soybean trypsin inhibitor complex and that the mechanism involves formation of an initial ternary complex followed by a time-dependent displacement of the proteinaceous inhibitor.

Original languageEnglish (US)
Pages (from-to)5105-5109
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number8
DOIs
StatePublished - Apr 16 2002

Fingerprint

Artificial Receptors
Serine Proteinase Inhibitors
Trypsin Inhibitors
Soybeans
Aprotinin
Chymotrypsin
Gel Chromatography
Electrophoresis
Proteins
Gels
Enzymes

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

@article{a537d99dff274a0e95834b5c64661dbf,
title = "Modulation of protein-protein interactions by synthetic receptors: Design of molecules that disrupt serine protease-proteinaceous inhibitor interaction",
abstract = "In the present article we describe the design and evaluation of a synthetic receptor that binds to the exterior surface of chymotrypsin and disrupts its interaction with proteinaceous inhibitors, such as soybean trypsin inhibitor, basic pancreatic trypsin inhibitor, ovomucoid turkey inhibitor, and Bowman-Birk inhibitor. Using enzyme kinetics, nondenaturing gel electrophoresis, and gel filtration chromatography we show that the receptor is particularly effective at blocking the chymotrypsin-soybean trypsin inhibitor complex and that the mechanism involves formation of an initial ternary complex followed by a time-dependent displacement of the proteinaceous inhibitor.",
author = "Park, {Hyung Soon} and Qing Lin and Andrew Hamilton",
year = "2002",
month = "4",
day = "16",
doi = "10.1073/pnas.082675899",
language = "English (US)",
volume = "99",
pages = "5105--5109",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "8",

}

TY - JOUR

T1 - Modulation of protein-protein interactions by synthetic receptors

T2 - Design of molecules that disrupt serine protease-proteinaceous inhibitor interaction

AU - Park, Hyung Soon

AU - Lin, Qing

AU - Hamilton, Andrew

PY - 2002/4/16

Y1 - 2002/4/16

N2 - In the present article we describe the design and evaluation of a synthetic receptor that binds to the exterior surface of chymotrypsin and disrupts its interaction with proteinaceous inhibitors, such as soybean trypsin inhibitor, basic pancreatic trypsin inhibitor, ovomucoid turkey inhibitor, and Bowman-Birk inhibitor. Using enzyme kinetics, nondenaturing gel electrophoresis, and gel filtration chromatography we show that the receptor is particularly effective at blocking the chymotrypsin-soybean trypsin inhibitor complex and that the mechanism involves formation of an initial ternary complex followed by a time-dependent displacement of the proteinaceous inhibitor.

AB - In the present article we describe the design and evaluation of a synthetic receptor that binds to the exterior surface of chymotrypsin and disrupts its interaction with proteinaceous inhibitors, such as soybean trypsin inhibitor, basic pancreatic trypsin inhibitor, ovomucoid turkey inhibitor, and Bowman-Birk inhibitor. Using enzyme kinetics, nondenaturing gel electrophoresis, and gel filtration chromatography we show that the receptor is particularly effective at blocking the chymotrypsin-soybean trypsin inhibitor complex and that the mechanism involves formation of an initial ternary complex followed by a time-dependent displacement of the proteinaceous inhibitor.

UR - http://www.scopus.com/inward/record.url?scp=0037117609&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037117609&partnerID=8YFLogxK

U2 - 10.1073/pnas.082675899

DO - 10.1073/pnas.082675899

M3 - Article

C2 - 11959960

AN - SCOPUS:0037117609

VL - 99

SP - 5105

EP - 5109

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 8

ER -