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Structural Investigation of Proapoptotic Peptide by Cd and Nmr Spectroscopy

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We have performed a systematic investigation of the structural features of the peptides Int (a sequence able to cross cell membranes) and Int-H1(S6A,F8A) (which shows interesting antitumoral properties). After screening in aqueous solution at different ionic strength and pH values, we analyzed the structures of the peptides in different water / trifluoroethanol mixtures by Circular Dichroism and Nuclear Magnetic Resonance techniques.

Keywords: circular dichroism; internalization sequence; molecular dynamics; nmr spectroscopy; proapoptotic sequence; trifluoroethanol

Document Type: Review Article


Affiliations: Department of Biophysical Sciences and Technologies M., University of Genoa, Europa 30, Genoa, Italy,Laboratory of Experimental Oncology, National Institute for Cancer Research, Largo R. Benzi 10, Genoa, Italy.

Publication date: December 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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