159610-89-6Relevant articles and documents
Noncovalent template-assisted mimicry of multiloop protein surfaces: Assembling discontinuous and functional domains
Ghosh, Partha S.,Hamilton, Andrew D.
, p. 13208 - 13211 (2012)
We report here a novel noncovalent synthetic strategy for template-assembled de novo protein design. In this approach, a peptide was first conjugated with two oligoguanosine strands via click chemistry and the conjugates were then self-assembled in the presence of metal ions. G-quadruplex formation directs two peptide strands to assemble on one face of the scaffold and form an adjacent two loop surface. This approach can be used to rapidly prepare multiple two-loop structures with both homo- and heterosequences.
Secondary-ion mass spectrometry of genetically encoded targets
Vreja, Ingrid C.,Saka, Sinem K.,Kr?hnert, Katharina,Opazo, Felipe,Rizzoli, Silvio O.,Kabatas, Selda,Diederichsen, Ulf,H?schen, Carmen
, p. 5784 - 5788 (2015)
Secondary ion mass spectrometry (SIMS) is generally used in imaging the isotopic composition of various materials. It is becoming increasingly popular in biology, especially for investigations of cellular metabolism. However, individual proteins are diffi
A combinatorial approach toward smart libraries of discontinuous epitopes of HIV gp120 on a TAC synthetic scaffold
Mulder, Gwenn E.,Kruijtzer, John A. W.,Liskamp, Rob M. J.
, p. 10007 - 10009,3 (2012)
We describe rapid and convenient access to smart libraries of protein surface discontinuous epitope mimics. Up to three different cyclic peptides, representing discontinuous epitopes in HIV-gp120, were conjugated to a triazacyclophane scaffold molecule via CuAAC. In this way protein mimics for use as synthetic vaccines and beyond will become available. This journal is
Synthesis of self-assembling cyclic peptide-polymer conjugates using click chemistry
Chapman, Robert,Jolliffe, Katrina A.,Perrier, Sebastien
, p. 1169 - 1172 (2010)
Self-assembling cyclic peptide-polymer conjugates were prepared by 'clicking' polymers (prepared by RAFT polymerization) to an azide functionalized d-alt-l cyclic octapeptide via the Huisgen 1,3-dipolar cycloaddition reaction. Due to the high graft density, the efficiency of the click chemistry conjugation reaction was found to be highly dependent on the size of the polymer. At relatively low molecular weights, as many as four polymer chains could be grafted to each 8 residue cyclic peptide ring. Evidence for the self assembly of the conjugates into peptide-polymer nanotubes was observed by TEM and IR. CSIRO 2010.
End-stapled homo and hetero collagen triple helices: A click chemistry approach
Byrne, Cillian,McEwan, Paul A.,Emsley, Jonas,Fischer, Peter M.,Chan, Weng C.
, p. 2589 - 2591 (2011)
A CuAAC reaction was established for modular synthesis of end-stapled homo- and hetero-triple helical peptides, generating "clicked" macro-assemblies with enhanced thermal stability.
Construction of tunable peptide nucleic acid junctions
Duan, Tanghui,He, Liu,Tokura, Yu,Liu, Xin,Wu, Yuzhou,Shi, Zhengshuang
, p. 2846 - 2849 (2018)
We report here the construction of 3-way and 4-way peptide nucleic acid (PNA) junctions as basic structural units for PNA nanostructuring. The incorporation of amino acid residues into PNA chains makes PNA nanostructures with more structural complexity and architectural flexibility possible, as exemplified by building 3-way PNA junctions with tunable nanopores. Given that PNA nanostructures have good thermal and enzymatic stabilities, they are expected to have broad potential applications in biosensing, drug delivery and bioengineering.
A Versatile Approach to Noncanonical, Dynamic Covalent Single- and Multi-Loop Peptide Macrocycles for Enhancing Antimicrobial Activity
Reuther, James F.,Goodrich, Andrew C.,Escamilla, P. Rogelio,Lu, Tiffany A.,Del Rio, Valarie,Davies, Bryan W.,Anslyn, Eric V.
, p. 3768 - 3774 (2018)
Peptide oligomers offer versatile scaffolds for the formation of potent antimicrobial agents due to their high sequence versatility, inherent biocompatibility, and chemical tunability. Though many methods exist for the formation of peptide-based macrocycles (MCs), increasingly pervasive in commercial antimicrobial therapeutics, the introduction of multiple looped structures into a single peptide oligomer remains a significant challenge. Herein, we report the utilization of dynamic hydrazone condensation for the versatile formation of single-, double-, and triple-loop peptide MCs using simple dialdehyde or dihydrazide small-molecule cross-linkers, as confirmed by MALDI-TOF MS, HPLC, and SDS-PAGE. Furthermore, incorporation of aldehyde-containing side chains onto peptides synthesized from hydrazide C-terminal resins resulted in tunable peptide MC assemblies formed directly upon resin cleavage post solid-phase peptide synthesis. Both of these types of dynamic covalent assemblies produced significant enhancements to overall antimicrobial properties when introduced into a known antimicrobial peptide, buforin II, when compared to the original unassembled sequence.
