Gold-phosphine binding to de novo designed coiled coil peptides

Research output: Contribution to journalArticle

Standard

Gold-phosphine binding to de novo designed coiled coil peptides. / Peacock, A.F.A.; Bullen, G.A.; Gethings, L.A.; Williams, J.P.; Kriel, F.H.; Coates, J.

In: Journal of Inorganic Biochemistry, Vol. 117, 01.12.2012, p. 298-305.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Peacock, A.F.A. ; Bullen, G.A. ; Gethings, L.A. ; Williams, J.P. ; Kriel, F.H. ; Coates, J. / Gold-phosphine binding to de novo designed coiled coil peptides. In: Journal of Inorganic Biochemistry. 2012 ; Vol. 117. pp. 298-305.

Bibtex

@article{81a1ab4331ed4516bd35f063e87e1742,
title = "Gold-phosphine binding to de novo designed coiled coil peptides",
abstract = "The coordination of the therapeutically interesting [AuCl(PEt)] to the de novo designed peptide, TRIL23C, under aqueous conditions, is reported here. TRIL23C represents an ideal model to investigate the binding of [AuCl(PEt)] to small proteins in an effort to develop novel gold(I) phosphine peptide adducts capable of mimicking biological recognition and targeting. This is due to the small size of TRIL23C (30 amino acids), yet stable secondary and tertiary fold, symmetric nature and the availability of only one thiol binding site. [AuCl(PEt)] was found to react readily with the Cys side chain in a 1:1 ratio as confirmed by UV-visible, P NMR and mass spectrometry. Circular dichroism confirmed that the coiled coil structure was retained on coordination of the {Au(PEt)} unit. Redesign of the exterior of TRIL23C based on a biologically relevant recognition sequence found in GCN4, did not alter the coordination chemistry of [AuCl(PEt)]. To the best of our knowledge, this represents the first report on the coordination of gold(I) phosphine compounds to de novo designed peptides, and could lead to the generation of novel gold(I) phosphine peptide therapeutics in the future.",
author = "A.F.A. Peacock and G.A. Bullen and L.A. Gethings and J.P. Williams and F.H. Kriel and J. Coates",
note = "Copyright 2012 Elsevier B.V., All rights reserved.",
year = "2012",
month = dec
day = "1",
doi = "10.1016/j.jinorgbio.2012.05.010",
language = "English",
volume = "117",
pages = "298--305",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Gold-phosphine binding to de novo designed coiled coil peptides

AU - Peacock, A.F.A.

AU - Bullen, G.A.

AU - Gethings, L.A.

AU - Williams, J.P.

AU - Kriel, F.H.

AU - Coates, J.

N1 - Copyright 2012 Elsevier B.V., All rights reserved.

PY - 2012/12/1

Y1 - 2012/12/1

N2 - The coordination of the therapeutically interesting [AuCl(PEt)] to the de novo designed peptide, TRIL23C, under aqueous conditions, is reported here. TRIL23C represents an ideal model to investigate the binding of [AuCl(PEt)] to small proteins in an effort to develop novel gold(I) phosphine peptide adducts capable of mimicking biological recognition and targeting. This is due to the small size of TRIL23C (30 amino acids), yet stable secondary and tertiary fold, symmetric nature and the availability of only one thiol binding site. [AuCl(PEt)] was found to react readily with the Cys side chain in a 1:1 ratio as confirmed by UV-visible, P NMR and mass spectrometry. Circular dichroism confirmed that the coiled coil structure was retained on coordination of the {Au(PEt)} unit. Redesign of the exterior of TRIL23C based on a biologically relevant recognition sequence found in GCN4, did not alter the coordination chemistry of [AuCl(PEt)]. To the best of our knowledge, this represents the first report on the coordination of gold(I) phosphine compounds to de novo designed peptides, and could lead to the generation of novel gold(I) phosphine peptide therapeutics in the future.

AB - The coordination of the therapeutically interesting [AuCl(PEt)] to the de novo designed peptide, TRIL23C, under aqueous conditions, is reported here. TRIL23C represents an ideal model to investigate the binding of [AuCl(PEt)] to small proteins in an effort to develop novel gold(I) phosphine peptide adducts capable of mimicking biological recognition and targeting. This is due to the small size of TRIL23C (30 amino acids), yet stable secondary and tertiary fold, symmetric nature and the availability of only one thiol binding site. [AuCl(PEt)] was found to react readily with the Cys side chain in a 1:1 ratio as confirmed by UV-visible, P NMR and mass spectrometry. Circular dichroism confirmed that the coiled coil structure was retained on coordination of the {Au(PEt)} unit. Redesign of the exterior of TRIL23C based on a biologically relevant recognition sequence found in GCN4, did not alter the coordination chemistry of [AuCl(PEt)]. To the best of our knowledge, this represents the first report on the coordination of gold(I) phosphine compounds to de novo designed peptides, and could lead to the generation of novel gold(I) phosphine peptide therapeutics in the future.

UR - http://www.scopus.com/inward/record.url?partnerID=yv4JPVwI&eid=2-s2.0-84869093025&md5=f31702b006e2fe4f18bda73f6a7ba751

U2 - 10.1016/j.jinorgbio.2012.05.010

DO - 10.1016/j.jinorgbio.2012.05.010

M3 - Article

AN - SCOPUS:84869093025

VL - 117

SP - 298

EP - 305

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

ER -