Relation between the activity of catalytic antibodies and the properties of substrates

Masato Kodaka, Anneli Hase

Research output: Contribution to journalArticleScientificpeer-review

1 Citation (Scopus)

Abstract

The free energy of binding between catalytic antibodies and substrates is correlated with the properties of the substrates, both in the transition state (TS) and the ground state (GS). The free energy of binding was calculated from the kinetic parameters and four properties of the substrates; the solvent accessible surface area (SAS), enthalpy of hydration (ΔH), polarizability (α), and dipole moment (μ) were calculated using AM1. As a whole, TS shows a higher correlation than does GS, which is compatible with the fundamental concept of a catalytic antibody. Among these four properties, SAS gives the highest correlation coefficient (0.7616) while μ has a small correlation. Antibody-TS complexes seem to be stabilized by van der Waals force rather than a hydrophobic interaction.
Original languageEnglish
Pages (from-to)3571-3574
Number of pages4
JournalBulletin of the Chemical Society of Japan
Volume69
Issue number12
DOIs
Publication statusPublished - 1996
MoE publication typeA1 Journal article-refereed

Fingerprint

Catalytic Antibodies
Electron transitions
Ground state
Free energy
Substrates
Van der Waals forces
Dipole moment
Kinetic parameters
Hydration
Enthalpy
Antibodies

Cite this

@article{7449263d7fb4422d8e5ebab65dca2de7,
title = "Relation between the activity of catalytic antibodies and the properties of substrates",
abstract = "The free energy of binding between catalytic antibodies and substrates is correlated with the properties of the substrates, both in the transition state (TS) and the ground state (GS). The free energy of binding was calculated from the kinetic parameters and four properties of the substrates; the solvent accessible surface area (SAS), enthalpy of hydration (ΔH), polarizability (α), and dipole moment (μ) were calculated using AM1. As a whole, TS shows a higher correlation than does GS, which is compatible with the fundamental concept of a catalytic antibody. Among these four properties, SAS gives the highest correlation coefficient (0.7616) while μ has a small correlation. Antibody-TS complexes seem to be stabilized by van der Waals force rather than a hydrophobic interaction.",
author = "Masato Kodaka and Anneli Hase",
year = "1996",
doi = "10.1246/bcsj.69.3571",
language = "English",
volume = "69",
pages = "3571--3574",
journal = "Bulletin of the Chemical Society of Japan",
issn = "0009-2673",
publisher = "The Chemical Society of Japan",
number = "12",

}

Relation between the activity of catalytic antibodies and the properties of substrates. / Kodaka, Masato; Hase, Anneli.

In: Bulletin of the Chemical Society of Japan, Vol. 69, No. 12, 1996, p. 3571-3574.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Relation between the activity of catalytic antibodies and the properties of substrates

AU - Kodaka, Masato

AU - Hase, Anneli

PY - 1996

Y1 - 1996

N2 - The free energy of binding between catalytic antibodies and substrates is correlated with the properties of the substrates, both in the transition state (TS) and the ground state (GS). The free energy of binding was calculated from the kinetic parameters and four properties of the substrates; the solvent accessible surface area (SAS), enthalpy of hydration (ΔH), polarizability (α), and dipole moment (μ) were calculated using AM1. As a whole, TS shows a higher correlation than does GS, which is compatible with the fundamental concept of a catalytic antibody. Among these four properties, SAS gives the highest correlation coefficient (0.7616) while μ has a small correlation. Antibody-TS complexes seem to be stabilized by van der Waals force rather than a hydrophobic interaction.

AB - The free energy of binding between catalytic antibodies and substrates is correlated with the properties of the substrates, both in the transition state (TS) and the ground state (GS). The free energy of binding was calculated from the kinetic parameters and four properties of the substrates; the solvent accessible surface area (SAS), enthalpy of hydration (ΔH), polarizability (α), and dipole moment (μ) were calculated using AM1. As a whole, TS shows a higher correlation than does GS, which is compatible with the fundamental concept of a catalytic antibody. Among these four properties, SAS gives the highest correlation coefficient (0.7616) while μ has a small correlation. Antibody-TS complexes seem to be stabilized by van der Waals force rather than a hydrophobic interaction.

U2 - 10.1246/bcsj.69.3571

DO - 10.1246/bcsj.69.3571

M3 - Article

VL - 69

SP - 3571

EP - 3574

JO - Bulletin of the Chemical Society of Japan

JF - Bulletin of the Chemical Society of Japan

SN - 0009-2673

IS - 12

ER -