1m02
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NMR Structure of PW2 Bound to SDS Micelles: A Tryptophan-rich Anticocidial Peptide Selected from Phage Display Libraries
OverviewOverview
PW2 (HPLKQYWWRPSI) was selected from phage display libraries through an, alternative panning method using living sporozoites of Eimeria acervulina, as target. Synthetic PW2 shows anticoccidial activity against E., acervulina and Eimeria tenella with very low hemolytic activity. It also, displays antifungal activity but no activity against bacteria. We present, the solution structure of the PW2 bound to SDS micelles. In the absence of, an interface, PW2 is in random coil conformation. In micelles, structural, calculation shows that Trp-7 forms the hydrophobic core that is important, for the peptide folding. Lys-4, Tyr-6, Trp-8, and Arg-9 are in the same, surface, possibly facing the micelle interface. This possibility was, supported by the fact that chemical shift differences for these residues, were more pronounced when compared with PW2 in water and in SDS. PW2 gains, structure upon binding to SDS micelles. Lys-4, Tyr-6, Trp-8, and Arg-9, were found to bind to the micelle. Trp-7, Trp-8, and Arg-9 composed the, WW+ consensus found in the sequence of the peptides selected with the, phage display technique against E. acervulina sporozoites. This suggested, that Trp-7, Trp-8, and Arg-9 are probably key residues not only for the, peptide interaction with SDS micelles but also for the interaction with E., acervulina sporozoites surface.
About this StructureAbout this Structure
1M02 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of PW2 bound to SDS micelles. A tryptophan-rich anticoccidial peptide selected from phage display libraries., Tinoco LW, Da Silva A Jr, Leite A, Valente AP, Almeida FC, J Biol Chem. 2002 Sep 27;277(39):36351-6. Epub 2002 Jul 18. PMID:12130641
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