Short peptide alpha helices induced by multiple metal clips

Hoang, Huy N., Bryant, Gavin K., Kelso, Micheal J., Beyer, Renee L., Appleton, Trevor G. and Fairlie, David P. (2003). Short peptide alpha helices induced by multiple metal clips. In: M. Sono and J. H. Dawson, Journal of Inorganic Biochemistry. Abstracts of the 11th International Conference on Biological Inorganic Chemistry. 11th International Conference on Biological Inorganic Chemistry, Cairns, Australia, (146-146). 19-23 July 2003. doi:10.1016/S0162-0134(03)80638-4


Author Hoang, Huy N.
Bryant, Gavin K.
Kelso, Micheal J.
Beyer, Renee L.
Appleton, Trevor G.
Fairlie, David P.
Title of paper Short peptide alpha helices induced by multiple metal clips
Conference name 11th International Conference on Biological Inorganic Chemistry
Conference location Cairns, Australia
Conference dates 19-23 July 2003
Proceedings title Journal of Inorganic Biochemistry. Abstracts of the 11th International Conference on Biological Inorganic Chemistry   Check publisher's open access policy
Journal name Journal of Inorganic Biochemistry   Check publisher's open access policy
Place of Publication New York, USA
Publisher Elsevier
Publication Year 2003
Sub-type Poster
DOI 10.1016/S0162-0134(03)80638-4
ISSN 0162-0134
1873-3344
Editor M. Sono
J. H. Dawson
Volume 96
Issue 1
Start page 146
End page 146
Total pages 1
Language eng
Abstract/Summary Alpha helices are key structural components of proteins and important recognition motifs in biology. New techniques for stabilizing short peptide helices could be valuable for studying protein folding, modeling proteins, creating artificial proteins, and may aid the design of inhibitors or mimics of protein function. We previously reported* that 5-15 residue peptides, corresponding to the Zn-binding domain of thermolysin, react with [Pd(en)(ONO,),]in DMF-d’ and 90% H,O 10% DzO to form a 22-membered [Pd(en)(H*ELTH*)]2+ macrocycle that is helical in solution and acts as a template in nucleating helicity in both Cand N- terminal directions within the longer sequences in DMF. ~f~~&g7$$& d&qx~m ~. y AC&q& In water, however, there was less a-helicity observed, testifying to #..q,& &$--Lb &l-- &.$;,J~p?:~~q&~+~~ ’ w w the difficulty of fixing intramolecular amide NH...OC H-bonds in 6,“;;” ( k.$ U”C.a , p d$. competition with the H-bond donor solvent water. To expand the utility of [Pd(en)(H*XXXH*)]*+ as a helix- @r4”8 & oJ#:& &G& @-qd ,‘d@-gyp promoting module in solution, we now report the result that Ac- ‘$4: %$yyy + H*ELTH*H*VTDH*-NH,(l), AC-H*ELTH*AVTDYH*ELTH*- NH, (2) and AC-H*AAAH*H*ELTH*H*VTDH*-NH* (3) react with multiple equivalents of [Pd(en)(ONO,),] to produce exclusively 4-6 respectively in both DMF-d7 and water (90% Hz0 10% D,O). Mass spectrometry, 15N- and 2D ‘H- NMR spectroscopy, and CD spectra were used to characterise the structures 4-6, and their three dimensional structures were calculated from NOE restraints using simulated annealing protocols. Results demonstrate (a) selective coordination of metal ions at (i, i+4) histidine positions in water and DMF, (b) incorporation of 2 and 3 a turn-mimicking modules [Pd(en)(HELTH)]2+ in lo-15 residue peptides, and (c) facile conversion of unstructured peptides into 3- and 4- turn helices of macrocycles, with well defined a-helicity throughout and more structure in DMF than in water.
Subjects CX
250204 Bioinorganic Chemistry
780103 Chemical sciences
Keyword Biochemistry & Molecular Biology
Chemistry, Inorganic & Nuclear
Q-Index Code CX

 
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Created: Wed, 15 Aug 2007, 02:43:19 EST