68280-74-0

Upstream product

• 2389-45-9 Boc-Lys(Z)-OH 
• 16652-71-4 benzyl (2S)-2-pyrrolidinecarboxylate hydrochloride 
• 84890-96-0 C₂₄H₃₆N₂O₈ 
• 41324-66-7 H-Pro-OBzl 
• 37787-77-2 Boc-L-proline benzyl ester 
• 100-51-6 benzyl alcohol 
• 147-85-3 L-proline 

Downstream Products

• 68280-75-1 benzyl N'-((benzyloxy)carbonyl)-L-lysyl-L-prolinate 
• 53157-73-6 Boc-Lys(Z)-Pro-OH 
• 68280-76-2 benzyl N⁶-((benzyloxy)carbonyl)-L-lysyl-L-prolinate trifluoroacetate 

Relevant academic research and scientific papers

Inhibition of urease enzyme activity by urea and thiourea derivatives of dipeptides conjugated 2, 3-dichlorophenyl piperazine

Objective: Studies on enzyme inhibition remain an important area of pharmaceutical research since these studies have led to the discoveries of drugs used in a variety of physiological conditions. In search of novel urease enzyme inhibitors, four dipeptide

Synthesis and bioactivity of a Goralatide analog with antileukemic activity

Natural tetrapeptide Goralatide (AcSDKP) is a selective inhibitor of primitive haematopoietic cell proliferation. It is not stable in vivo and decomposes within 4.5 min when applied to live cells. In this work we developed an analog of Goralatide that exhibits cytotoxicity towards human myeloid HL-60, HEL, Nalm-6 leukemia cells, endothelial HUVEC, glioblastoma U251 and transformed kidney 293T cells. The Goralatide analog showed significant stability in organic solution with no tendency to degrade oxidatively.

Solution-phase automated synthesis of tripeptide derivatives

An improved general method for automated synthesis of tripeptides was developed, in which methanesulfonic acid (MSA) was used in place of trifluoroacetic acid (TFA), thus making it possible to avoid, 1) corrosion of the apparatus by strong acid vapor, 2) formation of emulsions, and 3) use of the restricted solvent, dichloromethane. As an application of the automated synthesis apparatus, 216 fragment tripeptide derivatives were synthesized systematically using the MSA method, in excellent yield and with increased efficiency.

NAcSDKP analogues resistant to angiotensin-converting enzyme

Two series of analogues of the tetrapeptide NAcSDKP, an inhibitor of hematopoietic stem cell proliferation, were prepared, and their enzymatic stability toward rabbit lung angiotensin-converting enzyme (ACE) was evaluated as well as their capacity to inhibit NAcSDKP hydrolysis by this enzyme. In the first series, each of the peptide bonds has been successively replaced by an aminomethylene bond. In the second one, the C-terminus of the peptide has been modified by decarboxylation or amidation. The results reported here indicate that all of these molecules but one have good stability toward the enzyme but none of the compounds is able to inhibit NAcSDKP hydrolysis by ACE.

Synthesis and activity of NAcSerAspLysPro analogues on cellular interactions between T-cell and erythrocytes in rosette formation

Analogues of NAcSerAspLysPro (AcSDKP), a natural regulator of hematopoiesis isolated from fetal calf bone marrow, were synthesized. The biological activity of these molecules were evaluated in vitro in the rosette assay, which measures the interaction bet