scholarly journals Total synthesis of fellutamides, lipopeptide proteasome inhibitors. More sustainable peptide bond formation

2016 ◽  
Vol 14 (35) ◽  
pp. 8367-8375 ◽  
Author(s):  
Michael C. Pirrung ◽  
Fa Zhang ◽  
Sudhakar Ambadi ◽  
Y. Gangadhara Rao
Keyword(s):  
Natural Products ◽  
Total Synthesis ◽  
Bond Formation ◽  
Proteasome Inhibitors ◽  
Peptide Bond ◽  
Solution Phase ◽  
Peptide Bond Formation ◽  
Bioactive Natural Products

Solution-phase syntheses of three bioactive natural products of mixed polypeptide–polyketide biogenesis, fellutamides A, B, and C, have been achieved.

scholarly journals Correction: Total synthesis of fellutamides, lipopeptide proteasome inhibitors. More sustainable peptide bond formation

2016 ◽  
Vol 14 (38) ◽  
pp. 9159-9159
Author(s):  
Michael C. Pirrung ◽  
Fa Zhang ◽  
Sudhakar Ambadi ◽  
Y. Gangadhara Rao
Keyword(s):  
Total Synthesis ◽  
Bond Formation ◽  
Proteasome Inhibitors ◽  
Peptide Bond ◽  
Peptide Bond Formation

Correction for ‘Total synthesis of fellutamides, lipopeptide proteasome inhibitors. More sustainable peptide bond formation’ by Michael C. Pirrung, et al., Org. Biomol. Chem., 2016, 14, 8367–8375.

scholarly journals Evolutionary and functional analysis of an NRPS condensation domain integrates β-lactam, ᴅ-amino acid, and dehydroamino acid synthesis

2021 ◽  
Vol 118 (17) ◽  
pp. e2026017118
Author(s):  
Michael J. Wheadon ◽  
Craig A. Townsend
Keyword(s):  
Natural Products ◽  
Amino Acid ◽  
Bond Formation ◽  
Immediate Release ◽  
Peptide Bond ◽  
Sequence Motifs ◽  
Peptide Bond Formation ◽  
Specific Sequence ◽  
Dehydroamino Acid

Nonribosomal peptide synthetases (NRPSs) are large, multidomain biosynthetic enzymes involved in the assembly-line–like synthesis of numerous peptide natural products. Among these are clinically useful antibiotics including three classes of β-lactams: the penicillins/cephalosporins, the monobactams, and the monocyclic nocardicins, as well as the vancomycin family of glycopeptides and the depsipeptide daptomycin. During NRPS synthesis, peptide bond formation is catalyzed by condensation (C) domains, which couple the nascent peptide with the next programmed amino acid of the sequence. A growing number of additional functions are linked to the activity of C domains. In the biosynthesis of the nocardicins, a specialized C domain prepares the embedded β-lactam ring from a serine residue. Here, we examine the evolutionary descent of this unique β-lactam–synthesizing C domain. Guided by its ancestry, we predict and demonstrate in vitro that this C domain alternatively performs peptide bond formation when a single stereochemical change is introduced into its peptide starting material. Remarkably, the function of the downstream thioesterase (TE) domain also changes. Natively, the TE directs C terminus epimerization prior to hydrolysis when the β-lactam is made but catalyzes immediate release of the alternative peptide. In addition, we investigate the roles of C-domain histidine residues in light of clade-specific sequence motifs, refining earlier mechanistic proposals of both β-lactam formation and canonical peptide synthesis. Finally, expanded phylogenetic analysis reveals unifying connections between β-lactam synthesis and allied C domains associated with the appearance of ᴅ-amino acid and dehydroamino acid residues in other NRPS-derived natural products.

Formation of Carbon-Oxygen Bond Mediated by Hypervalent Iodine Reagents Under Metal-free Conditions

2020 ◽  
Vol 17 ◽  
Author(s):  
Ayesha Jalil ◽  
Yaxin O Yang ◽  
Zhendong Chen ◽  
Rongxuan Jia ◽  
Tianhao Bi ◽  
...  
Keyword(s):  
Natural Products ◽  
Bond Formation ◽  
Building Blocks ◽  
Review Article ◽  
Hypervalent Iodine ◽  
Metal Free ◽  
Bioactive Natural Products ◽  
The Past ◽  
Oxygen Bond ◽  
Privileged Scaffolds

: Hypervalent iodine reagents are a class of non-metallic oxidants have been widely used in the construction of several sorts of bond formations. This surging interest in hypervalent iodine reagents is essentially due to their very useful oxidizing properties, combined with their benign environmental character and commercial availability from the past few decades ago. Furthermore, these hypervalent iodine reagents have been used in the construction of many significant building blocks and privileged scaffolds of bioactive natural products. The purpose of writing this review article is to explore all the transformations in which carbon-oxygen bond formation occurred by using hypervalent iodine reagents under metal-free conditions

Beyond peptide bond formation: the versatile role of condensation domains in natural product biosynthesis

2021 ◽  
Author(s):  
Sofie Dekimpe ◽  
Joleen Masschelein
Keyword(s):  
Natural Product ◽  
Bond Formation ◽  
Peptide Bond ◽  
Chemical Diversity ◽  
Peptide Bond Formation ◽  
Natural Product Biosynthesis

Condensation domains perform highly diverse functions during natural product biosynthesis and are capable of generating remarkable chemical diversity.

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