Budisa N. Expanded genetic code for the engineering of ribosomally synthetized and post-translationally modified peptide natural products (RiPPs). Curr Opin Biotechnol. 2013;24:591–8.
Letzel AC, Pidot SJ, Hertweck C. Genome mining for ribosomally synthesized and post-translationally modified peptides (RiPPs) in anaerobic bacteria. BMC Genom. 2014;15:983.
Link AJ. Biosynthesis: leading the way to RiPPs. Nat Chem Biol. 2015;11:551–2.
Sardar D, Schmidt EW. Combinatorial biosynthesis of RiPPs: docking with marine life. Curr Opin Chem Biol. 2016;31:15–21.
Maksimov MO, Pan SJ, James Link A. Lasso peptides: structure, function, biosynthesis, and engineering. Nat Prod Rep. 2012;29:996–1006.
Cheung-Lee WL, Link AJ. Genome mining for lasso peptides: past, present, and future. J Ind Microbiol Biotechnol. 2019;46:1371–9.
Maksimov MO, Link AJ. Prospecting genomes for lasso peptides. J Ind Microbiol Biotechnol. 2014;41:333–44.
Hegemann JD, Zimmermann M, Xie X, Marahiel MA. Lasso peptides: an intriguing class of bacterial natural products. Acc Chem Res. 2015;48:1909–19.
Salomon RA, Farias RN. Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J Bacteriol. 1992;174:7428–35.
Solbiati JO, Ciaccio M, Farias RN, Salomon RA. Genetic analysis of plasmid determinants for microcin J25 production and immunity. J Bacteriol. 1996;178:3661–3.
Maksimov MO, Pelczer I, Link AJ. Precursor-centric genome-mining approach for lasso peptide discovery. Proc Natl Acad Sci USA. 2012;109:15223–8.
Tietz JI, et al. A new genome-mining tool redefines the lasso peptide biosynthetic landscape. Nat Chem Biol. 2017;13:470–8.
Jeanne Dit Fouque K, Bisram V, Hegemann JD, Zirah S, Rebuffat S, Fernandez-Lima F. Structural signatures of the class III lasso peptide BI-32169 and the branched-cyclic topoisomers using trapped ion mobility spectrometry-mass spectrometry and tandem mass spectrometry. Anal Bioanal Chem. 2019;411:6287–96.
Hegemann JD, et al. Xanthom*onins I-III: a new class of lasso peptides with a seven-residue macrolactam ring. Angew Chem Int Ed Engl. 2014;53:2230–4.
Hegemann JD, Zimmermann M, Zhu S, Klug D, Marahiel MA. Lasso peptides from proteobacteria: genome mining employing heterologous expression and mass spectrometry. Biopolymers. 2013;100:527–42.
Hegemann JD, Zimmermann M, Xie X, Marahiel MA. Caulosegnins I-III: a highly diverse group of lasso peptides derived from a single biosynthetic gene cluster. J Am Chem Soc. 2013;135:210–22.
Hegemann JD, Schwalen CJ, Mitchell DA, van der Donk WA. Elucidation of the roles of conserved residues in the biosynthesis of the lasso peptide paeninodin. Chem Commun. 2018;54:9007–10.
Cheung-Lee WL, et al. Discovery of ubonodin, an antimicrobial lasso peptide active against members of the Burkholderia cepacia complex. Chembiochem. 2019;21:1335–40.
Cheung-Lee WL, Parry ME, Jaramillo Cartagena A, Darst SA, Link AJ. Discovery and structure of the antimicrobial lasso peptide citrocin. J Biol Chem. 2019;294:6822–30.
Cheung-Lee WL, Cao L, Link AJ. Pandonodin: a proteobacterial lasso peptide with an exceptionally long C-terminal tail. ACS Chem Biol. 2019;14:2783–92.
Zimmermann M, Hegemann JD, Xie X, Marahiel MA. The astexin-1 lasso peptides: biosynthesis, stability, and structural studies. Chem Biol. 2013;20:558–69.
Martin-Gomez H, Linne U, Albericio F, Tulla-Puche J, Hegemann JD. Investigation of the biosynthesis of the lasso peptide chaxapeptin using an E. coli-based production system. J Nat Prod. 2018;81:2050–6.
Allen CD, Link AJ. Self-assembly of catenanes from lasso peptides. J Am Chem Soc. 2016;138:14214–7.
Zong C, Wu MJ, Qin JZ, Link AJ. Lasso peptide benenodin-1 is a thermally actuated [1] rotaxane switch. J Am Chem Soc. 2017;139:10403–9.
Koos JD, Link AJ. Heterologous and in vitro reconstitution of fuscanodin, a lasso peptide from Thermobifida fusca. J Am Chem Soc. 2019;141:928–35.
DiCaprio AJ, Firouzbakht A, Hudson GA, Mitchell DA. Enzymatic reconstitution and biosynthetic investigation of the lasso peptide fusilassin. J Am Chem Soc. 2019;141:290–7.
Kuroha M, Hemmi H, Ohnishi-Kameyama M, Kodani S. Isolation and structure determination of a new lasso peptide subterisin from Sphingomonas subterranea. Tetrahedron Lett. 2017;58:3429–32.
Kodani S, Hemmi H, Miyake Y, Kaweewan I, Nakagawa H. Heterologous production of a new lasso peptide brevunsin in Sphingomonas subterranea. J Ind Microbiol Biotechnol. 2018;45:983–92.
Hegemann JD, et al. Rational improvement of the affinity and selectivity of integrin binding of grafted lasso peptides. J Med Chem. 2014;57:5829–34.
Minoux H, Chipot C, Brown D, Maigret B. Structural analysis of the KGD sequence loop of barbourin, an αIIbβ3-specific disintegrin. J Comput Aided Mol Des. 2000;14:317–27.
Scarborough RM, et al. Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri. J Biol Chem. 1991;266:9359–62.
CAS PubMed Google Scholar
Horii A, Wang X, Gelain F, Zhang S. Biological designer self-assembling peptide nanofiber scaffolds significantly enhance osteoblast proliferation, differentiation and 3-D migration. PLoS ONE. 2007;2:e190.
Tsutsumi H, Kawamura M, Mihara H. Osteoblastic differentiation on hydrogels fabricated from Ca2+-responsive self-assembling peptides functionalized with bioactive peptides. Bioorg Med Chem. 2018;26:3126–32.
Scarborough RM, et al. Design of potent and specific integrin antagonists. Peptide antagonists with high specificity for glycoprotein IIb-IIIa. J Biol Chem. 1993;268:1066–73.
CAS PubMed Google Scholar
Yamada KM, Kennedy DW. Peptide inhibitors of fibronectin, laminin, and other adhesion molecules: unique and shared features. J Cell Physiol. 1987;130:21–28.
Hautanen A, Gailit J, Mann DM, Ruoslahti E. Effects of modifications of the RGD sequence and its context on recognition by the fibronectin receptor. J Biol Chem. 1989;264:1437–42.
CAS PubMed Google Scholar
Harada KI, Fujii K, Hayashi K, Suzuki M, Ikai Y, Oka H. Application of D,L-FDLA derivatization to determination of absolute configuration of constituent amino acids in peptide by advanced Marfey’s method. Tetrahedron Lett. 1996;37:3001–4.
Allen CD, Chen MY, Trick AY, Le DT, Ferguson AL, Link AJ. Thermal unthreading of the lasso peptides astexin-2 and astexin-3. ACS Chem Biol. 2016;11:3043–51.
Imbert M, Blondeau R. Effect of light on germinating spores of Streptomyces viridosporus. FEMS Microbiol Lett. 1999;181:159–63.
Kanie K, et al. Collagen type IV-specific tripeptides for selective adhesion of endothelial and smooth muscle cells. Biotechnol Bioeng. 2012;109:1808–16.
