Studies on Crystal Structure, Conformation Analysis ofa New Designed Hapten Containing Sulfur

Gui Yang Xie; Ya Li Kong; Jun Mei Wang; Xiao Jie Xu; Sheng Jin

Studies on Crystal Structure, Conformation Analysis ofa New Designed Hapten Containing Sulfur

Gui Yang Xie, Ya Li Kong, Jun Mei Wang, Xiao Jie Xu, Sheng Jin

Research output: Contribution to journal › Article › peer-review

Abstract

The crystal structure of a new designed hapten N-benzoyl tauryl phenylalanine was studied by XRD . The results showed that the configuration of sulfur atom is tetrahedron, -SO₂NH- is close to transition state of amide hydrolysis and there are several intermolecular hydrogen bonds. The crystal structure was optimized by Molgen program, and then compared with the hapten that contain phosphorus. The conformation analysis of N-S-C and N-P-C bonds showed that N-S-C had only one single low energy conformer. Their charges were also calculated by MOPAC program (AM1 calculation), and it is found that the charge distribution around S atom is very close to that of the P atom. Those results showed that the molecule could be used to induce antibodies with CPA activity.

Original language	English (US)
Pages (from-to)	893-894
Number of pages	2
Journal	Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities
Volume	20
Issue number	6
State	Published - Jun 10 1999

Keywords

Antibody enzyme
Hapten enzyme
Molecular design
Peptide hydrolysis

ASJC Scopus subject areas

General Chemistry

Cite this

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title = "Studies on Crystal Structure, Conformation Analysis ofa New Designed Hapten Containing Sulfur",

abstract = "The crystal structure of a new designed hapten N-benzoyl tauryl phenylalanine was studied by XRD . The results showed that the configuration of sulfur atom is tetrahedron, -SO2NH- is close to transition state of amide hydrolysis and there are several intermolecular hydrogen bonds. The crystal structure was optimized by Molgen program, and then compared with the hapten that contain phosphorus. The conformation analysis of N-S-C and N-P-C bonds showed that N-S-C had only one single low energy conformer. Their charges were also calculated by MOPAC program (AM1 calculation), and it is found that the charge distribution around S atom is very close to that of the P atom. Those results showed that the molecule could be used to induce antibodies with CPA activity.",

keywords = "Antibody enzyme, Hapten enzyme, Molecular design, Peptide hydrolysis",

author = "Xie, {Gui Yang} and Kong, {Ya Li} and Wang, {Jun Mei} and Xu, {Xiao Jie} and Sheng Jin",

year = "1999",

month = jun,

day = "10",

language = "English (US)",

volume = "20",

pages = "893--894",

journal = "Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities",

issn = "0251-0790",

publisher = "Higher Education Press Limited Company",

number = "6",

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TY - JOUR

T1 - Studies on Crystal Structure, Conformation Analysis ofa New Designed Hapten Containing Sulfur

AU - Xie, Gui Yang

AU - Kong, Ya Li

AU - Wang, Jun Mei

AU - Xu, Xiao Jie

AU - Jin, Sheng

PY - 1999/6/10

Y1 - 1999/6/10

N2 - The crystal structure of a new designed hapten N-benzoyl tauryl phenylalanine was studied by XRD . The results showed that the configuration of sulfur atom is tetrahedron, -SO2NH- is close to transition state of amide hydrolysis and there are several intermolecular hydrogen bonds. The crystal structure was optimized by Molgen program, and then compared with the hapten that contain phosphorus. The conformation analysis of N-S-C and N-P-C bonds showed that N-S-C had only one single low energy conformer. Their charges were also calculated by MOPAC program (AM1 calculation), and it is found that the charge distribution around S atom is very close to that of the P atom. Those results showed that the molecule could be used to induce antibodies with CPA activity.

AB - The crystal structure of a new designed hapten N-benzoyl tauryl phenylalanine was studied by XRD . The results showed that the configuration of sulfur atom is tetrahedron, -SO2NH- is close to transition state of amide hydrolysis and there are several intermolecular hydrogen bonds. The crystal structure was optimized by Molgen program, and then compared with the hapten that contain phosphorus. The conformation analysis of N-S-C and N-P-C bonds showed that N-S-C had only one single low energy conformer. Their charges were also calculated by MOPAC program (AM1 calculation), and it is found that the charge distribution around S atom is very close to that of the P atom. Those results showed that the molecule could be used to induce antibodies with CPA activity.

KW - Antibody enzyme

KW - Hapten enzyme

KW - Molecular design

KW - Peptide hydrolysis

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M3 - Article

AN - SCOPUS:0347138025

SN - 0251-0790

VL - 20

SP - 893

EP - 894

JO - Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities

JF - Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities

IS - 6

ER -

Studies on Crystal Structure, Conformation Analysis ofa New Designed Hapten Containing Sulfur

Abstract

Keywords

ASJC Scopus subject areas

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