@article { ISI:000336942100020,
	title = {Investigation of C-C bond formation mediated by bombyx mori silk fibroin materials},
	journal = {ACS Sustainable Chemistry \& Engineering},
	volume = {2},
	number = {6},
	year = {2014},
	month = {JUN},
	pages = {1510-1517},
	publisher = {AMER CHEMICAL SOC},
	address = {1155 16TH ST, NW, WASHINGTON, DC 20036 USA},
	abstract = {<p>The formation of C-C bonds is a prerequisite for all life on earth. Understanding the role of proteins in mediating the formation of these bonds is important for understanding biological mechanisms in evolution, as well as for designing {\textquoteleft}{\textquoteleft}green catalysts{\textquoteright}{\textquoteright}. In this work, the ability of silk fibroin (SF) proteins to mediate selective C-C bond formation under mild conditions was comprehensively evaluated and compared between different SF-based materials and other proteins. Aqueous SF solution (ASFS), freeze-dried SF (FDSF), mesoporous SF (MPSF), and SF hydrogel (SFHG) materials were prepared and characterized by a variety of techniques including, among others, FE-SEM, ICP-OES, FT-IR, and TGA. The nitroaldol (Henry) reaction, Knoevenagel condensation, and direct aldol reaction were used as models for this study, in which the recovery and reusability of the protein was also evaluated.</p>},
	keywords = {Aldol-like reactions, C-C Bond formation, Knoevenagel condensation, Proteins, Silk fibroin},
	issn = {2168-0485},
	doi = {10.1021/sc500184r},
	author = {Kuehbeck, Dennis and Ghosh, Munmun and Sen Gupta, Sayam and Diaz, David Diaz}
}
@article {46873,
	title = {Synthesis of phospho-polypeptides via phosphate-containing N-carboxyanhydride: application in enzyme-induced self-assembly, and calcium carbonate mineralization},
	journal = {ChemPlusChem},
	volume = {85},
	year = {2020},
	month = {MAY},
	pages = {1053-1064},
	type = {Article},
	abstract = {<p>An easy synthetic strategy was developed to synthesize the phosphate-functionalized amino acid N-carboxyanhydride (NCA), using simple primary amine initiators to obtain homo and block phospho-polypeptides with controlled molecular weight and molecular weight distribution. The methodology was extended to the synthesis of the end-functionalized homo polypeptides (15 to 50 repeat unit) and block co-polypeptides with PEG (0.7 K, 2 K, and 5 K) and glycopolypeptide (15-unit mannose glycopolypeptide) as one of the blocks. The deprotected fully water-soluble anionic phosphate-based polypeptides showed pH-dependent helical conformation with a helical content of 20 \%, which further changed to beta-sheets upon addition of the enzyme alkaline phosphatase (ALP) due to dephosphorylation. The block co-polypeptide containing PEG as one of the blocks led to its self-assembly into colloidal structures, such as vesicles with a hydrodynamic diameter of similar to 250 nm, due to the formation of amphiphilic block co-polymer upon dephosphorylation. The nature of the colloidal structures formed can be temporally controlled by the extent of dephosphorylation. Finally, the phospho-polypeptides serve as a template for the mineralization of calcium carbonate with varying polymorphs and morphologies.</p>
},
	keywords = {Biomineralization, enzymes, phosphopolypeptides, Proteins, Self-assembly},
	issn = {2192-6506},
	doi = {10.1002/cplu.202000322},
	author = {Mondal, Basudeb and Das, Soumen and Panda, Sidharth and Dutta, Tahiti and Sen Gupta, Sayam}
}
