Rapid nickel(ii)-promoted cysteine S-arylation with arylboronic acids

Abstract

Nickel salts catalyze fast cysteine arylation with 2-nitroarylboronic acids. The process uses cheap, readily-available reagents and allows introduction of diverse chemical handles.

Metal‐Mediated Functionalization of Natural Peptides and Proteins: Panning for Bioconjugation Gold

“…Residue-selective Asp [c] esterification with diazoacetyl derivative [76] Cu pepsin (41) 4 Asp, Glu, C-term metalation:r hodium(II) carboxylate exchange [181] Rh 33-mer peptide (3) 5.2 Cyst hioalkoxy-hydroxylation of allenes [33] Au RNase (14) 2.2 Cysp hotoredoxc ross-coupling of aryl halide [25] Ni 9-mer peptide (1) 2.1 Cysc oupling with preformed arylmetal complexes [78,87] Au, Pd antibody (150) 3.1,2 Cysi nsertion of diazo compounds into thiol SÀHbonds [133] Rh TIM (27) 4 Cysr eduction & metalation of disulfide site [190] Pt IgG (150) 5.5 CysC han-Lam coupling of 2-nitroaryl boronic acids [111] Ni B-domain from protein A(66) 3.5 Dha radical alkene addition using alkyl halides [30] Cu histone H3 (15) 2.2 His metalation:l igand binding to octahedralcomplex [161,221] Co,Rh a-thrombin (34) 5.1 Lysr eductive amination with aldehydes and formate [46] Ir lysozyme (14) 2.4 Lysc oupling with preformed arylmetal complexes [82] Pd 17-mer peptide (2) 3.1 Lysm etalation:s ubstitution on Fischer metallocarbene [192] Wl ysozyme (14) 5.6 Lysa zide formation by diazo transfer [135] Cu HRP (35) 4 N-term oxidative coupling via quinones pecies [38] Fe creatine kinase ( Chan-Lam coupling with arylboronic acids [104] Cu 12-mer peptide (1) 3.3 TrpC ÀHa rylation with aryliodinium reagents [71] Pd 3-mer peptide (1) 3.1 Trpm etallocarbene insertion with diazoacetates [127] Rh myoglobin (17) 4 Trpm etalation: h 6 -arene complexation [184] Ru 26-mer peptide (3) 5.3 TrpC ÀHe thynylation with an alkynyliodine(III) reagent [89] Au myoglobin (17) 3.2 Tyro xidative coupling via acyclic diazene [40] Fe antibody (150) 2.3 Tyr [e] oxidative coupling via atyrosyl radical [21,22] Ni, Ru gp32 (34) 2.1, 6.…”

“…Moving away from common palladium or copper catalysts,B all and co-workers recently reported that asimple nickel(II) salt can induce rapid cysteine arylation with a2 -nitroarylboronic acid (Figure 18). [111] Ther eaction is fast:1 0-30 min is sufficient for quantitative modification under mild reaction conditions (aqueous buffer, 37 8 8C). Oxidized disulfides are unreactive, but pretreatment with ar eductant (TCEP) allowed modification of oxidized cysteinet argets.I nterestingly, ortho substituents with resonance-based electron-withdrawing character are essential for reactivity,aprofile that differs significantly from backbone modification with copper(II) (Section 3.3) and, indeed, from Chan-Lam coupling in general, [92][93][94] which points to am echanistic pathway distinct from standard Chan-Lam coupling.S ome protein substrates (e.g.…”

Metallvermittelte Funktionalisierung natürlicher Peptide und Proteine: Biokonjugation mit Übergangsmetallen

“…[111] schiede zu den Rückgratmodifikationen mit Kupfer(II)-(Abschnitt 3.3) und natürlich der Chan-Lam-Kupplung im Allgemeinen auf, [92][93][94] was insgesamt auf einen mechanistischen Pfad abseits der typischen Chan-Lam-Kupplung hindeutet. Ball und Mitarbeiter rückten kürzlich von herkçmmlichen Palladium-oder Kupferkatalysatoren ab und publizierten die Induktion einer schnellen Cysteinarylierung durch ein einfaches Nickel(II)-Salz, bei der 2-Nitroarylboronsäure als Reagenz zum Einsatz kam (Abbildung 18).…”

“…CysT hioalkoxyhydroxylierung von Allenen [33] Au RNase (14) 2.2 CysP hotoredox-Kreuzkupplung von Arylhalogeniden [25] Ni 9-mer-Peptid (1) 2.1 CysK upplung mit vorgeformten Arylmetallkomplexen [78,87] Au, Pd Antikçrper (150) 3.1,2 CysT hiol-S-H-Insertion von Diazoverbindungen [133] Rh TIM (27) 4 CysR eduktion & Metallierung an Disulfidzentren [190] Pt IgG (150) 5.5 CysC han-Lam-Kupplung mit 2-Nitroaryl boronsäuren [111] Ni B-Domäne aus Protein A(66) 3.5 Dha…”

Copper-mediated peptide arylation selective for the N-terminus

“…Cross-coupling reactivity, typically mediated by transition metal complexes, have become important tools for N-C bond formation, and they represent an interesting approach to selective modication of peptides and proteins. [3][4][5][6][7] Chemoselective cysteine coupling has been achieved with a variety of transition metal-mediated approaches, [8][9][10][11] and tyrosine is selectively modied with p-allyl intermediates. 12 In contrast, cross-coupling at amine groups in polypeptides are limited to a few special cases, including arylpalladium reagents that mediate arylation of lysine side chains in non-aqueous solvents 13 and arylation of individual amino acid derivatives with Cu [14][15][16] or Pd, 17,18 typically at elevated temperatures under non-aqueous conditions.…”