68802-90-4Relevant academic research and scientific papers
Plasmin-Binding Tripeptide-Decorated Liposomes Loading Pyrazolo[3,4- d]pyrimidines for Targeting Hepatocellular Carcinoma
Calandro, Pierpaolo,Iovenitti, Giulia,Zamperini, Claudio,Candita, Francesca,Dreassi, Elena,Chiariello, Mario,Angelucci, Adriano,Schenone, Silvia,Botta, Maurizio,Mancini, Arianna
, p. 646 - 651 (2018)
Hepatocellular carcinoma (HCC) is one of the most fatal cancer types worldwide. HCC cells were proved to overexpress c-Src and Sgk1, a tyrosine and a serine-threonine kinase, respectively, whose role is crucial for the development and progression of the tumor. Pyrazolo[3,4-d]pyrimidine derivatives are a class of tyrosine kinase inhibitors that have shown good activity against HepG2. HCC cells were also proved to overexpress plasmin, which is localized on the cell surface bound to its receptors. In this study, a tripeptide with sequence d-Ala-Phe-Lys, which binds a specific reactive site of plasmin, was synthesized and characterized. This tripeptide was used to decorate liposomes encapsulating three selected pyrazolo[3,4-d]pyrimidines. Liposomes bearing tripeptide have been characterized, not showing remarkable differences with respect to the corresponding tripeptide-free liposomes. In vitro HepG2 cell uptake profiles and cytotoxicities showed that the presence of the tripeptide on the liposomal membrane surface improves the cell-penetrating ability of liposomes and increases the activity of two of the three tested compounds.
Stimuli-responsive supramolecular gelation in ferrocene-peptide conjugates
Afrasiabi, Rouzbeh,Kraatz, Heinz-Bernhard
supporting information, p. 17296 - 17300 (2014/01/06)
Teaching an old dog new tricks: Ferrocene-dipeptide conjugates capable of forming gels in response to various external signals including sound, thermal, redox, and mechanical stress are reported (see figure). Interesting examples of how ferrocene-peptide conjugates can be exploited for the construction of organometallic gelators are demonstrated.
Synthesis of sansalvamide A peptidomimetics: Triazole, oxazole, thiazole, and pseudoproline containing compounds
Davis, Melinda R.,Singh, Erinprit K.,Wahyudi, Hendra,Alexander, Leslie D.,Kunicki, Joseph B.,Nazarova, Lidia A.,Fairweather, Kelly A.,Giltrap, Andrew M.,Jolliffe, Katrina A.,McAlpine, Shelli R.
experimental part, p. 1029 - 1051 (2012/02/15)
Peptidomimetic-based macrocycles typically have improved pharmacokinetic properties over those observed with peptide analogs. Described are the syntheses of 13 peptidomimetic derivatives that are based on active sansalvamide A structures, where these analogs incorporate heterocycles (triazoles, oxazoles, thiazoles, or pseudoprolines) along the macrocyclic backbone. The syntheses of these derivatives employ several approaches that can be applied to convert a macrocyclic peptide into its peptidomimetic counterpart. These approaches include peptide modifications to generate the alkyne and azide for click chemistry, a serine conversion into an oxazole, a Hantzsch reaction to generate the thiazole, and protected threonine to generate the pseudoproline derivatives. Furthermore, we show that two different peptidomimetic moieties, triazoles, and thiazoles, can be incorporated into the macrocyclic backbone without reducing cytotoxicity: triazole and thiazole.
Engineered Thermoplasma acidophilum factor F3 mimics human aminopeptidase N (APN) as a target for anticancer drug development
Su, Jing,Wang, Qiang,Feng, Jinhong,Zhang, Cong,Zhu, Deyu,Wei, Tiandi,Xu, Wenfang,Gu, Lichuan
scheme or table, p. 2991 - 2996 (2011/06/21)
Human aminopeptidase N (hAPN) is an appealing objective for the development of anti-cancer agents. The absence of mammalian APN experimental structure negatively impinges upon the progression of structure-based drug design. Tricorn interacting factor F3 (factor F3) from Thermoplasma acidophilum shares 33% sequence identity with hAPN. Engineered factor F3 with two point directed mutations resulted in a protein with an active site identical to hAPN. In the present work, the engineered factor F3 has been co-crystallized with compound D24, a potent APN inhibitor introduced by our lab. Such a holo-form experimental structure helpfully insinuates a more bulky pocket than Bestatin-bound Escherichia coli APN. This evidence discloses that compound D24 targetting the structure of E. coli APN cannot bind to the activity cleft of factor F3 with high affinity. Thus, there is a potential risk of inefficiency to design hAPN targeting drug while using E. coli APN as the target model. We do propose here now that engineered factor F3 can be employed as a reasonable alternative of hAPN for drug design and development.
TRIPEPTIDE DERIVATIVES AND ANTIPLASMIN AGENTS CONTAINING THE SAME
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, (2008/06/13)
Tripeptide derivatives of the formula:A--aaa(B)--Phe--Lys--C (I)wherein A, B and C are each one of a specific range of substituents, and aaa, Phe and Lys are each of a specific range of amino acid residues, are potent inhibitors of plasmin and useful for
