MASS SPECTROMETRIC CHARACTERIZATION OF SOME GEL-FORMING PEPTIDES

Peptide-based hydrogels have become an area of intense investigation due to their easy design, possibility to make a large range of hierarchical nanostructures and their high biocompatibility and biodegradability. Here, we investigated by mass spectrometry (MS) a few synthetic gel-forming peptides having different amino acid sequences. Four different peptides were selected for MS measurements: EEEOH, FFFFF-OH, FESNF-NH2, and LWMRFA-OH. get detailed information on structure, molecular weight, and chemical bond energies of gel-forming peptides as well as to assess their purity and stability. Fourier transform infrared spectroscopy (FTIR) and ChemDraw Ultra computer programs confirmed the MS data. The peptide tendency to aggregate, a process observed by MS in the case of peptide EEE in a polar environment, was also theoretically investigated by molecular modeling.