IR study of TFA unpurified synthetic peptides in aqueous solutions. TFA removal and band assignment

LAURA E. VALENTI; MAXIMILIANO BURGOS PACI; CARLOS P. DE PAULI; CARLA E. GIACOMELLI

ACADEMIC PRESS INC ELSEVIER SCIENCE

Año: 2011 vol. 410 p. 118 - 118

font size="1" face="AdvGulliv-R"> Synthetic peptide or protein samples are mostly unpurified with trifluoroacetic acid (TFA) used during the synthesis procedure, which strongly interferes with structure determination by infrared (IR) spectroscopy. The aim of this work was to propose a simple strategy to remove TFA contribution from attenuated total reflection (ATR)–IR spectra of the hexahistidine peptide (His6) in aqueous solution to study the conformation of this synthetic peptide without previous purification. Such a strategy is based on the subtraction mode widely employed to remove water contribution, and it is tested with TFA unpurified histidine as a model system. The subtraction is based on eliminating the strong TFA bands at 1147 and 1200 cm