Protein–polymer conjugates prepared via host–guest interactions: effects of the conjugation site, polymer type and molecular weight on protein activity

2016 ◽  
Vol 7 (32) ◽  
pp. 5139-5146 ◽  
Author(s):  
Limin Cao ◽  
Xiujuan Shi ◽  
Yuecheng Cui ◽  
Weikang Yang ◽  
Gaojian Chen ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Activity ◽  
Polymer Conjugates ◽  
Protein Polymer ◽  
P Protein ◽  
Polymer Type

Protein–polymer conjugates are prepared via host–guest interactions and the effects of various parameters on protein activity are investigated.

scholarly journals Mapping protein–polymer conformations in bioconjugates with atomic precision

2020 ◽  
Vol 11 (24) ◽  
pp. 6160-6166 ◽  
Author(s):  
Kevin M. Burridge ◽  
Ben A. Shurina ◽  
Caleb T. Kozuszek ◽  
Ryan F. Parnell ◽  
Jonathan S. Montgomery ◽  
...  
Keyword(s):  
Magnetic Resonance ◽  
Polymer Conjugates ◽  
Protein Polymer ◽  
P Protein ◽  
Atomic Precision

Protein–polymer conjugates are explored using magnetic resonance methods to investigate the conformations of the polymer relative to the protein's surface.

Visible light induced fast synthesis of protein–polymer conjugates: controllable polymerization and protein activity

2014 ◽  
Vol 50 (49) ◽  
pp. 6506-6508 ◽  
Author(s):  
Xin Li ◽  
Lei Wang ◽  
Gaojian Chen ◽  
David M. Haddleton ◽  
Hong Chen
Keyword(s):  
Visible Light ◽  
Ambient Temperature ◽  
Raft Polymerization ◽  
Protein Activity ◽  
Polymer Conjugates ◽  
Protein Polymer ◽  
Novel Method ◽  
Fast Synthesis

Visible light induced fast and controllable RAFT polymerization from protein as a novel method for preparing protein–polymer conjugates at ambient temperature.

On the immunological properties of penicillins

1971 ◽  
Vol 179 (1057) ◽  
pp. 411-432 ◽  
Keyword(s):  
Proteolytic Enzyme ◽  
Continuous Process ◽  
Polymeric Materials ◽  
Small Peptides ◽  
Physiological Conditions ◽  
Polymer Conjugates ◽  
Protein Polymer ◽  
Penicillanic Acid ◽  
Insoluble Form ◽  
Polyvalent Antigens

Penicilloylated proteins which may be found as impurities in 6-amino-penicillanic acid can be exhaustively digested by pronase to yield amino acids and small peptides. This degradation converts the potent polyvalent antigens into a mixture of mostly monovalent haptens which are much less immunogenic and less capable of eliciting immune reactions in sensitized animals. In order to avoid the contamination of 6-aminopenicillanic acid with a proteolytic enzyme, pronase was converted into a water insoluble form by coupling it with bromoacetyl cellulose. This insoluble derivative of pronase retains its activity and broad specificity. It can be readily removed from the medium upon completion of the impurity degradation, to be used repeatedly in a continuous process. The immunological manifestations associated with penicillins are not completely abolished by removal or degradation of protein impurities. Another important cause for these manifestations appears to be polymeric materials which are formed in penicillins. Such polymeric materials were isolated from ampicillin and shown to be capable of binding spontaneously to proteins (e.g. bovine serum albumin). The protein-polymer conjugates, which are formed under physiological conditions (pH 7.4, 37 °C), were found to be immunogenic and to provoke the formation of polymer-specific antibodies.

scholarly journals Crosslinking of Self-Assembled Protein–Polymer Conjugates with Divanillin

2020 ◽  
Author(s):  
Zihao Li ◽  
Yanyan Jiang ◽  
Kilian Wüst ◽  
Manuela Callari ◽  
Martina H. Stenzel
Keyword(s):  
Polymer Conjugates ◽  
Protein Polymer ◽  
Self Assembled

scholarly journals Synthetic approach to homodimeric protein–polymer conjugates

2009 ◽  
pp. 2148 ◽  
Author(s):  
Lei Tao ◽  
Catherine S. Kaddis ◽  
Rachel R. Ogorzalek Loo ◽  
Gregory N. Grover ◽  
Joseph A. Loo ◽  
...  
Keyword(s):  
Synthetic Approach ◽  
Polymer Conjugates ◽  
Protein Polymer
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