22221-61-0Relevant academic research and scientific papers
Mechanoresponsive, proteolytically stable and biocompatible supergelators from ultra short enantiomeric peptides with sustained drug release propensity
Basu, Anindya,Christman, Ryann M.,Duttkonar, Anita,Harjit, Jeena,Mehra, Radha Rani,Mishra, Anil K.,Tiwari, Amit K.
, p. 6346 - 6354 (2020)
Stimuli-responsive low molecular weight hydrogelators attract immense interest from diverse segments of biomedicine and biotechnology. Distinctly, herein we report newly synthesized enantiomeric ultrashort peptides of general formula Me-(CH2)8-CO-NH-CH(X)-COOH, where X = CH2Ph in hydrogelators I (l-Phe) and II (d-Phe) respectively, which display excellent self-assembling propensity in physiological buffer at room temperature. Interestingly these biomolecules were endowed with mechanoresponsiveness, injectability and high mechanical integrity as confirmed by rheological measurements. Importantly they revealed resistance towards proteolytic degradation. Indeed dose dependent cell viability studies using MTT assay in four different cell lines, namely PANC-1, S1, HCT-116 and MDAMB-231, further confirmed the biocompatibility of the hydrogelators in vitro. The structural aspect of β-sheets of the hydrogelators was concluded on the basis of temperature dependent NMR, IR, PXRD and computational studies. We developed a user friendly delivery system, hydrogel nanoparticles (HNPs), with our mechanoresponsive and biocompatible hydrogelators, as these particles exhibited promising influence due to their enhanced surface area. Also the HNPs revealed excellent drug release kinetics for the model drugs 5FU/doxorubicin under physiological conditions in a sustained manner depending on the physicochemical parameters of the drugs. Taking these results together we envision that our designed hydrogelators and the delivery vehicle generated therefrom might represent a promising tool for administration of significant drug concentrations at lesion sites for a prolonged period, thus providing a better strategy for quick pain relief, rapid recovery and reduced systemic side effects.
Synthesis and biochemical investigation of scyphostatin analogues as inhibitors of neutral sphingomyelinase
Arenz,Gartner,Wascholowski,Giannis
, p. 2901 - 2904 (2007/10/03)
The sphingolipid ceramide is considered to be an important intracellular mediator. However, many aspects of its action and the role of several different ceramide generating sphingomyelinases are still unclear. Recently, we reported on the synthesis of the first selective irreversible inhibitor of the neutral sphingomyelinase (N-SMase), as well as the identification of Manumycin A and some of its analogues as irreversible inhibitors of N-SMase. For the development of pharmacologically interesting competitive inhibitors of N-SMase, structure-activity studies are essential. Herein we show the synthesis and enzymatic investigation of two scyphostatin analogues 3a and 3b, revealing the importance of the primary hydroxy group in compound 2 for N-SMase inhibition.
Novel stereoselective incorporation and hydrolysis of long-chain amino-acid substrates by vesicular membrane systems which include tri- or tetra-peptide catalysts
Ohkubo, Katsutoshi,Urabe, Kenji,Yamamoto, Junji,Sagawa, Takashi,Usui, Satoshi
, p. 2957 - 2960 (2007/10/03)
In the vesicular membrane system comprising N,N-didodecyl-N,N-dimethylammonium bromide and tri- and or tetra-peptide catalysts (pH 7.68; ionic strength μ = 0.15; 298 K), Z-L-Leu-L-His-L-Leu (or Z-L-Leu-L-His-L-Leu-L-Leu), having a hydrophobic terminal L-l
Enantioselective Hydrolysis of N-Acyl Amino Acid Esters by Tripeptide-type L-Histidine Derivative in a Bilayer Vesicular System
Ohkubo, Katsutoshi,Ishida, Hitoshi,Yamaki, Kazuhiro,Kawata, Masahiko
, p. 1723 - 1726 (2007/10/02)
Peculiar enantioselective hydrolysis of N-acyl amino acid esters was found in the bilayer vesicular systems containing the tripeptide-type histidine derivative, Z-L-Leu-L-His-L-Leu.The enantioselectivity for the hydrolysis of long chain N-acyl phenylalanine p-nitrophenyl ester, C16-Phe-PNP, appeared in the binding process and was governed by an entropy factor.
Enantioselective Catalysis of Deacylation of p-Nitrophenyl N-Acylphenylalanates by Mixed Micelles composed of Nα-Hexadecanoyl-L-histidine and a Cationic Surfactant
Ueoka, Ryuichi,Murakami, Yukito
, p. 219 - 224 (2007/10/02)
The deacylation of p-nitrophenyl N-acyl-L and -D-phenylalanates (acyl=acetyl, decanoyl, and hexadecanoyl) with the co-micellar system composed of Nα-hexadecanoyl-L-histidine and octadecyltrimethylammonium chloride was investigated for the 20-35
STEREOSELECTIVE DEACYLATION OF LONG-CHAIN p-NITROPHENYL N-ACYLPHENYLALANATES BY PALMITOYL-L-HISTIDINE IN A BILAYER SYSTEM
Ueoka, Ryuichi,Matsumoto, Yoko,Ninomiya, Yashushi,Nakagawa, Yoshiharu,Inoue, Kazuhiro,Ohkubo, Katsutoshi
, p. 785 - 788 (2007/10/02)
In the stereoselective deacylation of H-n-1 -CONHCH(CH2Ph)CO2-C6H4NO2-p (n=10 and 16), the bilayer catalytic systems of palmitoyl-L-histidine and double-chain surfactants (2N2Br; m=12 and 14) offered the relatively higher enantiomer rat
