Trishomocubane amino acid as a β-turn scaffold

被引：23

作者：

Albericio, Fernando

Arvidson, Per I. ^{[2
,3
]}

Bisetty, Krishna ^{[4
]}

Giral, Ernest

Govender, Thavendran ^{[5
]}

Jali, Samuel ^{[1
]}

Kongsaeree, Palangpon ^{[6
,7
]}

Kruger, Hendrik G. ^{[1
]}

Prabpai, Samran ^{[6
,7
]}

机构：

[1] Univ Kwazulu Natal, Sch Chem, ZA-4041 Durban, South Africa

[2] Univ Barcelona, Dept Organ Chem, E-08028 Barcelona, Spain

[3] Uppsala Univ, Dept Biochem & Organ Chem, S-75123 Uppsala, Sweden

[4] Durban Inst Technol, Dept Chem, ZA-4000 Durban, South Africa

[5] Univ Kwazulu Natal, Sch Pharm, ZA-4041 Durban, South Africa

[6] Mahidol Univ, Dept Chem, Bangkok 10400, Thailand

[7] Mahidol Univ, Ctr Prot Struct & Funct, Bangkok 10400, Thailand

来源：

CHEMICAL BIOLOGY & DRUG DESIGN | 2008年 / 71卷 / 02期

关键词：

AMBER; beta-turn; cage peptide; trishomocubane amino acid; X-ray structure;

D O I：

10.1111/j.1747-0285.2007.00618.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The synthesis and X-ray structure of two diasteriomeric heptapeptides [Ac-Ala-Ala-Ala-(R/S)-Cage-Ala-Ala-Ala-NH2] with a trishomocubane amino acid as a beta-turn scaffold are reported. The amino acid was synthesized as a racemate and two diastereomeric peptides were obtained. The two peptides were separated by preparative high-pressure liquid chromatography and crystals suitable for X-ray analysis were grown for both diasteriomeric peptides. In general, both the peptides satisfy the criteria for beta-turn conformations. Five of the six Ala residues of both cage peptide crystals satisfy the criteria for 3(10)-helix characteristics and the cage amino acid residue satisfied the m-helix classification. These experimental results confirm previous theoretical studies in our laboratory which predicted that the cage moiety would be a strong/active beta-turn inducer.

引用

页码：125 / 130

页数：6

共 57 条

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