Synthesis and bioactivity of pyrrole-conjugated phosphopeptides

• Qiuxin Zhang,
• Weiyi Tan and
• Bing Xu

Beilstein J. Org. Chem. 2022, 18, 159–166, doi:10.3762/bjoc.18.17

• ][11], collagen mimic [12], antibacterial [13][14], biomineralization [15][16], mimicry of amyloids [17], cell cultures [18], and tissue engineering [19]. Particularly, the use of enzyme-instructed self-assembly (EISA) [20][21] of peptide assemblies has expanded the applications of peptide assemblies

Enzyme-instructed morphological transition of the supramolecular assemblies of branched peptides

• Dongsik Yang,
• Hongjian He and
• Bing Xu

Beilstein J. Org. Chem. 2020, 16, 2709–2718, doi:10.3762/bjoc.16.221

• ][20][21][22][23][24][25][26], as mimicry of amyloids [27], in the context of intracellular phase transition [28], and in molecular imaging [29][30]. Most of these studies are centered on peptide amphiphiles or amphiphilic peptides that are linear in geometry. Nature, however, also produces and

Inhibition of peptide aggregation by means of enzymatic phosphorylation

• Kristin Folmert,
• Malgorzata Broncel,
• Hans v. Berlepsch,
• Christopher H. Ullrich,
• Mary-Ann Siegert and
• Beate Koksch

Beilstein J. Org. Chem. 2016, 12, 2462–2470, doi:10.3762/bjoc.12.240

• protofilaments and on to insoluble amyloid fibrils, and we found a remarkable directing effect from β-sheet-rich structures to unfolded structures in the initial growth phase, in which small oligomers and protofilaments prevail if the peptide is phosphorylated. Keywords: aggregation; amyloids; peptide models

• with biological function with desirable mechanical properties. Many such peptide aggregates display exceptional stability, mechanical strength, stability at high temperatures and they are resistant towards enzymatic degradation [2]. Several studies have demonstrated the utilization of amyloids as

• form amyloids [59][60]. The recognition site for PKA is located next to the aggregation domain of KFM6, with just three amino acids distance to the phosphorylated serine residue. The short distance to this hydrophobic aggregation domain could enable an interaction with the polar phosphate group

A journey in bioinspired supramolecular chemistry: from molecular tweezers to small molecules that target myotonic dystrophy

• Steven C. Zimmerman

Beilstein J. Org. Chem. 2016, 12, 125–138, doi:10.3762/bjoc.12.14

• and thereby: (1) inhibit the toxicity of amyloidogenic proteins in cell culture, (2) modulate Aβ protein oligomerization, and (3) disintegrate preformed Aβ fibrils [35]. CLR01 (20) was recently shown capable of antagonizing seminal amyloids involved in HIV infection [36]. Beyond the impressive

Assembly of synthetic Aβ miniamyloids on polyol templates

• Sebastian Nils Fischer and
• Armin Geyer

Beilstein J. Org. Chem. 2015, 11, 2646–2653, doi:10.3762/bjoc.11.284

• template 16 to obtain threefold boronic ester 17. The miniamyloid 17 assembles from seven components by imine and boronic ester bonds between the peptides and the template. The relative orientation and spacing of the peptides mimic the assembly of peptides in Alzheimer β-amyloids. Keywords: Alzheimer

• , such as those forming amyloids. The solubility of the assembly should be maintained throughout the experiment and precipitation strictly avoided to reach the thermodynamic equilibrium with the formation of the most stable miniamyloid in solution. Not all functional groups listed above for the

• minor signal sets in the proton 1H NMR spectra. Detailed analytical studies of 17 and its possible functional mimicry of toxic Aβ amyloids, according to our previous study of irreversibly covalently linked miniamyloids, are under progress. Conclusion In conclusion, we presented a strategy which merges