scholarly journals Self-assembled biomimetic architectures : protein-polymer conjugates and lipid-polymer hybrids for biomedical applications

2018 ◽  
Author(s):  
◽  
Amit Kumar Khan
Keyword(s):  
Biomedical Applications ◽  
Polymer Conjugates ◽  
Protein Polymer ◽  
Polymer Hybrids ◽  
Self Assembled

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

Self-assembled nanostructures from amphiphilic globular protein–polymer hybrids

2017 ◽  
Vol 75 (6) ◽  
pp. 2627-2639 ◽  
Author(s):  
Qi Cao ◽  
Naipu He ◽  
Yue Wang ◽  
Zhenwu Lu
Keyword(s):  
Globular Protein ◽  
Protein Polymer ◽  
Polymer Hybrids ◽  
Self Assembled

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.

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