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Titolo:
Caerin 4.1, an antibiotic peptide from the Australian tree frog, Litoria caerulea. The NMR-derived solution structure
Autore:
Chia, BCS; Carver, JA; Lindner, RA; Bowie, JH; Wong, H; Lie, W;
Indirizzi:
Univ Adelaide, Dept Chem, Adelaide, SA 5005, Australia Univ Adelaide Adelaide SA Australia 5005 em, Adelaide, SA 5005, Australia Univ Wollongong, Dept Chem, Wollongong, NSW 2522, Australia Univ Wollongong Wollongong NSW Australia 2522 ongong, NSW 2522, Australia Ind Res Ltd, Lower Hutt, New Zealand Ind Res Ltd Lower Hutt New ZealandInd Res Ltd, Lower Hutt, New Zealand AgRes, Wallaceville Anim Res Ctr, Upper Hutt, New Zealand AgRes Upper Hutt New Zealand ille Anim Res Ctr, Upper Hutt, New Zealand
Titolo Testata:
AUSTRALIAN JOURNAL OF CHEMISTRY
fascicolo: 4, volume: 53, anno: 2000,
pagine: 257 - 265
SICI:
0004-9425(2000)53:4<257:C4AAPF>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
SECONDARY STRUCTURE; CHEMICAL-SHIFTS; SKIN GLANDS; H-1;
Keywords:
circular dichroism; double quantum filtered correlation spectroscopy; heteronuclear single-quantum coherence; minimum inhibitory concentration; nuclear Overhauser effect spectroscopy; restrained molecular dynamics; root mean square deviation; simulated annealing; trifluoroethanol; total correlation spectroscopy; one- and two-dimensional;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Chia, BCS Univ Adelaide, Dept Chem, Adelaide, SA 5005, Australia Univ Adelaide Adelaide SA Australia 5005 de, SA 5005, Australia
Citazione:
B.C.S. Chia et al., "Caerin 4.1, an antibiotic peptide from the Australian tree frog, Litoria caerulea. The NMR-derived solution structure", AUST J CHEM, 53(4), 2000, pp. 257-265

Abstract

Caerin 4.1 (GLWQK(5)IKSAA(10)GDLAS(15)GIEVG(20)IKS-NH2) is an antibiotic peptide isolated from the Australian tree frog Litoria caerulea. Unlike caerin 1.1, the major peptide isolated from this species, caerin 4.1 has a narrow spectrum of antibiotic activity, e.g. it shows selective activity against Pasteurella haemolytica and Escherichia coli. Caerin 4.1 consists of 23 amino acid residues and is comparable in size with other wide-spectrum antibiotic peptides isolated from Australian amphibians, e.g. caerin 1.1 and maculatin 1.1. An n.m.r. study in trifluoroethanol/water indicates that caerin4.1 forms an amphipathic alpha-helix with distinct hydrophilic and hydrophobic zones. Two regions of well defined helicity (from Gln4 to Ala10 and from Ile17 to Ile21) are separated by a central helical region of greater conformational variability. The enhanced disorder in this region arises from the presence of two central glycine residues at positions 11 and 16. However, the degree of disorder and hence flexibility is much less than in caerin 1.1 where central proline residues are present instead. This reduced central flexibility may account for the narrow spectrum of biological activity ofcaerin 4.1, i.e. because biological membranes of the various bacteria havedifferent composition and topology, their optimal interaction with the relatively rigid caerin 4.1 peptide is not possible.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 21:22:41