Dataset Information

Light-Up of Rhodamine Hydrazide to Generate Emissive Initiator for Polymerization and to Afford Photochromic Polypeptide Metal Complex.

ABSTRACT: Ring-opening polymerization (ROP) of cyclic peptide monomer of ?-propargyl-l-glutamate N-carboxyanhydride (PLG?NCA) was originally initiated by non-emissive, ring-close rhodamine 6G hydrazide (R-C). However, instantaneously after adding PLG?NCA to R-C, the spirolactam ring of R-C was opened by PLG?NCA, rendering emissive, ring-open R-O to initiate ROP of PLG?NCA. The emissive R-O moiety therefore produced fluorescent R?PLG with aggregation-induced emission (AIE) properties. Moreover, R?PLG was found to exhibit photochromic properties with good fatigue resistance and long lifetime when forming metal complexes with Sn(II) and Fe(III). In the dark, irradiated metal complexes slowly (~50 min) restored to the initial state. This research provides foundation for the development of new photochromic materials with long lifetime.

SUBMITTER: Gao JY

PROVIDER: S-EPMC6418603 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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Publications

Light-Up of Rhodamine Hydrazide to Generate Emissive Initiator for Polymerization and to Afford Photochromic Polypeptide Metal Complex.

Gao Jhen-Yan JY Huang Wen-Chih WC Huang Pei-Yi PY Song Cheng-Yu CY Hong Jin-Long JL

Polymers 20170905 9

Ring-opening polymerization (ROP) of cyclic peptide monomer of γ-propargyl-l-glutamate N-carboxyanhydride (PLG⁻NCA) was originally initiated by non-emissive, ring-close rhodamine 6G hydrazide (R-C). However, instantaneously after adding PLG⁻NCA to R-C, the spirolactam ring of R-C was opened by PLG⁻NCA, rendering emissive, ring-open R-O to initiate ROP of PLG⁻NCA. The emissive R-O moiety therefore produced fluorescent R⁻PLG with aggregation-induced emission (AIE) properties. Moreover, R⁻PLG was f ...[more]

PMID: 30965719

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Project description:Initiation of plasmid rolling circle replication (RCR) is catalyzed by a plasmid-encoded Rep protein that performs a Tyr- and metal-dependent site-specific cleavage of one DNA strand within the double-strand origin (dso) of replication. The crystal structure of RepB, the initiator protein of the streptococcal plasmid pMV158, constitutes the first example of a Rep protein structure from RCR plasmids. It forms a toroidal homohexameric ring where each RepB protomer consists of two domains: the C-terminal domain involved in oligomerization and the N-terminal domain containing the DNA-binding and endonuclease activities. Binding of Mn2+ to the active site is essential for the catalytic activity of RepB. In this work, we have studied the effects of metal binding on the structure and thermostability of full-length hexameric RepB and each of its separate domains by using different biophysical approaches. The analysis of the temperature-induced changes in RepB shows that the first thermal transition, which occurs at a range of temperatures physiologically relevant for the pMV158 pneumococcal host, represents an irreversible conformational change that affects the secondary and tertiary structure of the protein, which becomes prone to self-associate. This transition, which is also shown to result in loss of DNA binding capacity and catalytic activity of RepB, is confined to its N-terminal domain. Mn2+ protects the protein from undergoing this detrimental conformational change and the observed protection correlates well with the high-affinity binding of the cation to the active site, as substituting one of the metal-ligands at this site impairs both the protein affinity for Mn2+and the Mn2+-driven thermostabilization effect. The level of catalytic activity of the protein, especially in the case of full-length RepB, cannot be explained based only on the high-affinity binding of Mn2+ at the active site and suggests the existence of additional, lower-affinity metal binding site(s), missing in the separate catalytic domain, that must also be saturated for maximal activity. The molecular bases of the thermostabilizing effect of Mn2+ on the N-terminal domain of the protein as well as the potential location of additional metal binding sites in the entire RepB are discussed.

Dataset Information

Light-Up of Rhodamine Hydrazide to Generate Emissive Initiator for Polymerization and to Afford Photochromic Polypeptide Metal Complex.

Publications

Light-Up of Rhodamine Hydrazide to Generate Emissive Initiator for Polymerization and to Afford Photochromic Polypeptide Metal Complex.

Similar Datasets

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