76379-00-5

Upstream product

• 100-02-7 4-nitro-phenol 
• 117997-81-6 5-(benzyloxy)-2-(tert-butoxycarbonylamino)-5-oxopentanoic acid 
• 41840-28-2 S-tert-butoxycarbonyl-4,6-dimethyl-2-mercaptopyrimidine 
• 2578-33-8 D-glutamic acid-5-benzyl ester 
• 35793-73-8 N-(tert-butyloxycarbonyl)-γ-benzyl-D-glutamic acid 

Downstream Products

• 98926-82-0 (R)-4-tert-Butoxycarbonylamino-4-dodecylcarbamoyl-butyric acid benzyl ester 
• 120059-63-4 Boc-D-Glu(OBzl)-Tyr-Nle-D-Lys(Z)-Trp-Nle-Asp-Phe-NH₂ 
• 18800-73-2 benzyl (R)-5-amino-4-((tert-butoxycarbonyl)amino)-5-oxopentanoate 
• 80143-17-5 (R)-1-amino-5-(benzyloxy)-1,5-dioxopentan-2-aminium 2,2,2-trifluoroacetate 
• 18814-49-8 tert-butoxycarbonyl-L-alanyl-D-isoglutamine benzyl ester 
• 66111-49-7 t-butoxycarbonyl-L-valyl-D-isoglutamine benzyl ester 
• 63091-92-9 N-t-butyloxycarbonyl-O-benzyl-L-seryl-D-isoglutamine benzyl ester 
• 62853-36-5 L-alanyl-(γ-benzyl ester D-isoglutamine) 
• 71811-15-9 tert-butoxycarbonyl-α-aminoisobutyryl-D-isoglutamine benzyl ester 
• 56772-92-0 muramyl dipeptide 
• 71811-14-8 D-Glutaminsaeure-α-amid-γ-benzylester 
• 71811-16-0 (R)-4-(2-Amino-2-methyl-propionylamino)-4-carbamoyl-butyric acid benzyl ester 
• 45159-25-9 L-alanyl-D-isoglutamine 
• 74221-14-0 L-valyl-D-isoglutamine benzyl ester 

Relevant academic research and scientific papers

Activation for catalysis of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus by bacterial cell wall

Methicillin-resistant Staphylococcus aureus (MRSA) has acquired a unique penicillin-binding protein (PBP), PBP 2a, which has rendered the organism resistant to the action of all available β-lactam antibiotics. The X-ray structure of PBP 2a shows the active site in a closed conformation, consistent with resistance to inhibition by β-lactam antibiotics. However, it is known that PBP 2a avidly cross-links the S. aureus cell wall, which is its physiological function. It is shown herein that synthetic fragments of the bacterial cell wall bind in a saturable manner to PBP 2a and cause a conformational change in the protein that makes the active site more accessible to binding to a β-lactam antibiotic. These observations and measurements point to a novel strategy by nature to keep the active site of PBP 2a sheltered from the inhibitory activity of the antibiotics, yet it becomes available to the polymeric cell wall by a requisite conformational change for the critical cell wall cross-linking reaction. Copyright

SYNTHESIS OF POLY(ETHYLENE GLYCOL) BLOCK COPOLYMERS AS POTENTIAL WATER-SOLUBLE DRUG CARRIERS

The synthesis of a model water-soluble drug carrier based on poly(ethylene glycol) (PEG) block copolymers is described.In the copolymers, two blocks of PEG are linked by a biodegradable oligopeptide or amino acid linkage containing the glutamic acid residue. 4-Nitroaniline as a drug model is attached to the γ-carboxyl group of glutamic acid of the polymer carrier via an enzymatically degradable oligopeptide spacer.The oligopeptides used were potential substrates for chymotrypsin.The relationship between the structure of oligopeptides linking two PEG blocks and the rate of chymotrypsin-catalyzed polymer chain degradation as well as the relationship between the structure of the spacer and kinetics of drug model release from the carrier after incubation of chymotrypsin solution is discussed in detail.The results showed that by modifying the structure of oligopeptides in the polymer construct, changes in the rates of both polymer degradation and the drug model release can be achieved in a very broad range.