Examining the Polyproline Nanoscopic Ruler in the Context of Quantum Dots

Autor:	James B. Delehanty, Joseph S. Melinger, Kelly Boeneman Gemmill, Kimihiro Susumu, Juan B. Blanco-Canosa, David A. Hastman, Philip E. Dawson, Igor L. Medintz, Thomas Pons, Stella H. North, Eunkeu Oh, Michael H. Stewart, Ashok A. Deniz, Hsiao-Wei Liu, Sebastián A. Díaz, Jeffrey R. Deschamps
Rok vydání:	2015
Předmět:	chemistry.chemical_classification Chemistry General Chemical Engineering Peptide General Chemistry Acceptor Fluorescence Crystallography Förster resonance energy transfer Semiconductor quantum dots Quantum dot Materials Chemistry Nanoscopic scale Polyproline helix
Zdroj:	Chemistry of Materials. 27:6222-6237
ISSN:	1520-5002 0897-4756
DOI:	10.1021/acs.chemmater.5b03181
Popis:	The rigidity and defined length of the polyproline type II helix (PPII) have made it the structural basis of a nanoscopic ruler, which has been widely applied in Forster resonance energy transfer (FRET) studies. A growing body of data, however, has questioned the foundation for this and has provided evidence for structural perturbations to the PPII caused by temperature, salt content, solvent polarity, and even Pro repeat length. Here, we examine the polyproline ruler in the context of semiconductor quantum dots (QDs) and FRET. For this study, a series of polyproline peptides (Pron, n = 0, 3, 6, 9, 12, 15, 18) displaying a C-terminal hexahistidine sequence (His6) and an N-terminal cysteine for site-specific labeling with Cy3 dye were synthesized. Peptide rigidity was first examined with ATTO 647 Ni2+-nitrilotriacetic acid acceptor dye coordinated to the His6-termini of the Cy3 donor-labeled peptides. These conditions provided a steady-state fluorescent response that closely followed FRET predictions deriv...
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::81bca4d262dec8dda142f7557bcc1df5 https://doi.org/10.1021/acs.chemmater.5b03181 Zobrazit plný text záznamu