Year-end Sale % OFF 
Abstract
Protein nanomaterials at the peptide level have shown great potential for medical applications. Peptides change their morphological conformation because of changes in self-assembly properties when they are exposed to changes in solvent composition or pH. Two 15-residue peptide sequences, KhK (KKKFLIVIGSIIKKK) and Alternating Kh (KFLKKIVKIGKKSII), were designed for the purpose of determining the role of peptide sequence on solution morphology and conformation. KhK solutions exhibited a random coil to helical transition when solvent conditions were changed from water to a trifluorethanol/water solution at acidic pH. Alternating Kh solutions, however, demonstrated primarily random coil character under similar solvent and pH conditions as determined by circular dichroism spectroscopy and 2D-1H-1H nuclear magnetic resonance spectroscopy. At basic pH, circular dichroism spectroscopy and nuclear magnetic resonance spectroscopy analysis demonstrated that random coil character increased at basic pH for KhK, whereas Alternating Kh exhibited an increase in beta-sheet character. Further analysis by transmission electron microscopy showed marked differences in the peptide solution morphology. Peptide particle aggregation and fiber formation were significantly affected by solvent composition and pH values for both peptide sequences.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
