applications of circular dichroism for structural analysis of gelatin and antimicrobial peptides圆二色性的应用明胶和抗菌肽的结构分析.pdfVIP

Int. J. Mol. Sci. 2012, 13, 3229-3244; doi:10.3390/ijm OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 /journal/ijms Article Applications of Circular Dichroism for Structural Analysis of Gelatin and Antimicrobial Peptides Ramamourthy Gopal 1, Jin Soon Park 2, Chang Ho Seo 3 and Yoonkyung Park 2,* 1 Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea; E-Mail: ramagopa@ 2 Department of Biotechnology, Chosun University, Gwangju 501-759, Korea; E-Mail: jsmw2001@ 3 Department of Bioinformatics, Kongju National University, Kongju, South Korea; E-Mail: chseo@kongju.ac.kr * Author to whom correspondence should be addressed; E-Mail: y_k_park@chosun.ac.kr; Tel.: +82-62-230-6854; Fax: +82-62-225-6758. Received: 31 January 2012; in revised form: 2 March 2012 / Accepted: 5 March 2012 / Published: 8 March 2012 Abstract: Circular dichroism (CD) is a useful technique for monitoring changes in the conformation of antimicrobial peptides or gelatin. In this study, interactions between cationic peptides and gelatin were observed without affecting the triple helical content of the gelatin, which was more strongly affected by anionic surfactant. The peptides did not adopt a secondary structure in the presence of aqueous solution or Tween 80, but a peptide secondary structure formed upon the addition of sodium dodecyl sulfate (SDS). The peptides bound to the phos