74844-91-0Relevant articles and documents
Construction of Challenging Proline-Proline Junctions via Diselenide-Selenoester Ligation Chemistry
Sayers, Jessica,Karpati, Phillip M. T.,Mitchell, Nicholas J.,Goldys, Anna M.,Kwong, Stephen M.,Firth, Neville,Chan, Bun,Payne, Richard J.
, p. 13327 - 13334 (2018)
Polyproline sequences are highly abundant in prokaryotic and eukaryotic proteins, where they serve as key components of secondary structure. To date, construction of the proline-proline motif has not been possible owing to steric congestion at the ligatio
C3′-endo-puckered pyrrolidine containing PNA has favorable geometry for RNA binding: Novel ethano locked PNA (ethano-PNA)
Banerjee, Anjan,Kumar, Vaijayanti A.
, p. 4092 - 4101 (2013)
A novel peptide nucleic acid (PNA) analogue is designed with a constraint in the aminoethyl segment of the aegPNA backbone so that the dihedral angle β is restricted within 60-80, compatible to form PNA:RNA duplexes. The designed monomer is further functionalized with positively charged amino-/guanidino-groups. The appropriately protected monomers were synthesized and incorporated into aegPNA oligomers at predetermined positions and their binding abilities with cDNA and RNA were investigated. A single incorporation of the modified PNA monomer into a 12-mer PNA sequence resulted in stronger binding with complementary RNA over cDNA. No significant changes in the CD signatures of the derived duplexes of modified PNA with complementary RNA were observed.
Design and synthesis of fluorinated peptides for analysis of fluorous effects on the interconversion of polyproline helices
Li, Meng-Che,Liu, Ying-Jie,Hsu, Kuang-Cheng,Lin, Tse-Hsueh,Lin, Chih-Wei,Horng, Jia-Cherng,Wang, Sheng-Kai
, (2021/11/30)
The unique interaction between fluorine atoms has been exploited to alter protein structures and to develop synthetic and analytical applications. To expand such fluorous interaction for novel applications, polyproline peptides represent an excellent molecular nanoscaffold for controlling the presentation of perfluoroalkyl groups on their unique secondary structure. We develop approaches to synthesis fluorinated peptides to systematically investigate how the number, location and types of the fluorous groups on polyproline affect the conformation by monitoring the transition between the two major polyproline structures PPI and PPII. This work provides valuable information on how fluorous interaction affects the peptide structure and also benefits the design of functional fluorous molecules.
Quinoline-Proline, Triazole Hybrids: Design, Synthesis, Antituberculosis, Molecular Docking, and ADMET Studies
Ganesan, Moorthiamma Sarathy,Raja, Kamatchi Kanmani,Murugesan, Sankaranarayanan,Karankumar, Banoth,Faheem, Faheem,Thirunavukkarasu, Sappanimuthu,Shetye, Gauri,Ma, Rui,Franzblau, Scott G.,Wan, Baojie,Rajagopal, Gurusamy
, p. 952 - 968 (2021/02/16)
A series of novel quinoline-proline hybrids (11a-g) and quinoline-proline-1,2,3-triazole hybrids (12-14) were synthesized by click chemistry based on molecular hybridization concept and were characterized by NMR, mass spectrometry, and elemental analysis. All the titled target compounds were tested for antitubercular activity by MABA and LORA methods by in vitro. Interestingly, two compounds (2R,4S)-1-((2-cyclopropyl-4-(4-fluorophenyl)-quinolin-3-yl)-methyl)-4-(4-nitrobenzamido)-N-phenylpyrrolidine-2-carboxamide (11b) and (2R,4S)-1-((2-cyclopropyl-4-(4-fluorophenyl)-quinolin-3-yl)-methyl)-4-(4-fluorobenzamido)-N-phenylpyrrolidine-2-carboxamide (11c) exhibited significant activity against the tested Mycobacterium tuberculosis H37Rv strain. Further, the cytotoxicity (CC50) profile of the titled compounds against the Vero cell was performed and discussed. A molecular docking study of the hit compounds (11b and 11c) was also performed to find their putative binding interaction with the active site of the target proteins. Finally, in silico ADMET properties were also predicted for all the synthesized molecules to evaluate their drug-likeness behavior.
Multipodal insulin mimetics built on adamantane or proline scaffolds
Hajduch, Jan,Fabre, Benjamin,Klopp, Benjamin,Pohl, Radek,Budě?ínsky, Milo?,?olínová, Veronika,Ka?i?ka, Václav,K?prülüoglu, Cemal,Eyrilmez, Saltuk Mustafa,Lep?ík, Martin,Hobza, Pavel,Mitrová, Katarína,Lubos, Marta,Hernández, María Soledad Garre,Jirá?ek, Ji?í
, (2020/12/29)
Multi-orthogonal molecular scaffolds can be applied as core structures of bioactive compounds. Here, we prepared four tri-orthogonal scaffolds based on adamantane or proline skeletons. The scaffolds were used for the solid-phase synthesis of model insulin mimetics bearing two different peptides on the scaffolds. We found that adamantane-derived compounds bind to the insulin receptor more effectively (Kd value of 0.5 μM) than proline-derived compounds (Kd values of 15–38 μM) bearing the same peptides. Molecular dynamics simulations suggest that spacers between peptides and central scaffolds can provide greater flexibility that can contribute to increased binding affinity. Molecular modeling showed possible binding modes of mimetics to the insulin receptor. Our data show that the structure of the central scaffold and flexibility of attached peptides in this type of compound are important and that different scaffolds should be considered when designing peptide hormone mimetics.
