Nmr-Study on a Sryd-Containing Fibronectin-Like Sequence-(250-257) of Leishmania-Gp63 - Contribution of Residual Water in the Dimethyl-Sulfoxide Solution Structure (Journal article)

Tsikaris, V./ Cung, M. T./ Sakarellos, C./ Tzinia, A. K./ Soterladou, K. P./ Sakarellos-Daitsiotis, M.

The conformational characteristics of the I(250)ASRYDQL(257) synthetic octapeptide, which incorporates the SRYD adhesion site (252-255) of Leishmania gp63, have been investigated at pH 2 and 5, by means of 1D and 2D H-1 NMR spectroscopy (temperature coefficient values, chemical shifts, vicinal coupling constants and NOE effects). It was found that elimination of residual water from the dimethyl sulfoxide (DMSO) solution at pH 2 provides exchange peaks in the ROESY and HOHAHA spectra similar to those obtained for the DMSO peptide solution at pH 5. This common structure is stabilized (i) by the formation of a type I beta-turn involving the QNH --> RCO interaction and (ii) by a possible interaction between the guanidinium and the D-beta-carboxylate groups. After treatment with molecular sieves, the remaining residual water is redistributed between the peptide functional groups and participates in the rigidification of the new conformational state.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: cell-adhesion,spectroscopy,peptides,region,rgd
URI: https://olympias.lib.uoi.gr/jspui/handle/123456789/8597
ISSN: 0300-9580
Link: <Go to ISI>://A1994NF45100028
Publisher: Royal Society of Chemistry
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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