Aqueous ROPISA of ?-amino acid <i>N</i>-carboxyanhydrides: polypeptide block secondary structure controls nanoparticle shape anisotropy
نویسندگان
چکیده
Ring-Opening Polymerization-Induced Self-Assembly (ROPISA) of N -carboxyanhydride is an efficient one-step process to obtain nanomaterials made polypeptides.
منابع مشابه
Large-scale synthesis of α-amino acid-N-carboxyanhydrides
Heteroand homopolymers prepared from α-amino acid-N-carboxyanhydrides (NCAs) monomers are widely useful products. The preparation of pure NCA monomers has been extensively studied in the past. Purification methods including repeated crystallizations, extraction, and flash column chromatography have been devised. However, these methods are not easily amendable to large-scale NCA preparations. Th...
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Methodology has been developed for the general synthesis of optically active beta-amino acid N-carboxyanhydrides (beta-NCAs) through cyclization of N(beta)-Boc or N(beta)-Cbz beta-amino acids using phosphorus tribromide. The formation of beta-NCAs was confirmed by spectroscopy as well as an X-ray structural determination of beta-homoalanine-N-carboxyanhydride. The beta-NCA molecules could be po...
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The correlations of primary and secondary structures were analyzed using proteins with known structure from Protein Data Bank. The correlation values of amino acid type and the eight secondary structure types at distant position were calculated for distances between -25 and 25. Shapes of the diagrams indicate that amino acids polarity and capability for hydrogen bonding have influence on the se...
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The amino acid sequence of cystatin, the protein from chicken egg-white that is a tight-binding inhibitor of many cysteine proteinases, is reported. Cystatin is composed of 116 amino acid residues, and the Mr is calculated to be 13 143. No striking similarity to any other known sequence has been detected. The results of computer analysis of the sequence and c.d. spectrometry indicate that the s...
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Three equivocal amino acid sequences were synthesized that are predicted to be alpha-helical from amino acid preference but are found to be primarily beta-strand from x-ray diffraction of their respective proteins. In some solvent systems we recover the alpha-helical structure predicted by amino acid preference, whereas in other systems we mimic the interior of the protein and produce a beta-st...
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ژورنال
عنوان ژورنال: Polymer Chemistry
سال: 2021
ISSN: ['1759-9962', '1759-9954']
DOI: https://doi.org/10.1039/d1py00995h