Selective Bi‐directional Amide Bond Cleavage of<i>N</i>‐Methylcysteinyl Peptide

Qiu, Yibo; Hemu, Xinya; Liu, Ding Xiang

doi:10.1002/ejoc.201402261

Cited by 5 publications

(2 citation statements)

References 60 publications

(31 reference statements)

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“…To exploit cyclotides and cyclic knottins for agricultural and medical use, it is necessary to develop efficient methods for their production. Methods employed to date include solid phase peptide synthesis [ 9 , 211 , 222 , 223 , 224 , 225 , 226 , 227 ], as well as chemo-enzymatic and biological methods using modified inteins [ 210 , 211 , 212 , 213 ] and Asn-endoprotease such as butelase-1 [ 228 , 229 , 230 , 231 ].…”

Section: Classification and Characteristicsmentioning

confidence: 99%

Antimicrobial Peptides from Plants

et al. 2015

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Plant antimicrobial peptides (AMPs) have evolved differently from AMPs from other life forms. They are generally rich in cysteine residues which form multiple disulfides. In turn, the disulfides cross-braced plant AMPs as cystine-rich peptides to confer them with extraordinary high chemical, thermal and proteolytic stability. The cystine-rich or commonly known as cysteine-rich peptides (CRPs) of plant AMPs are classified into families based on their sequence similarity, cysteine motifs that determine their distinctive disulfide bond patterns and tertiary structure fold. Cystine-rich plant AMP families include thionins, defensins, hevein-like peptides, knottin-type peptides (linear and cyclic), lipid transfer proteins, α-hairpinin and snakins family. In addition, there are AMPs which are rich in other amino acids. The ability of plant AMPs to organize into specific families with conserved structural folds that enable sequence variation of non-Cys residues encased in the same scaffold within a particular family to play multiple functions. Furthermore, the ability of plant AMPs to tolerate hypervariable sequences using a conserved scaffold provides diversity to recognize different targets by varying the sequence of the non-cysteine residues. These properties bode well for developing plant AMPs as potential therapeutics and for protection of crops through transgenic methods. This review provides an overview of the major families of plant AMPs, including their structures, functions, and putative mechanisms.

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Section: Classification and Characteristicsmentioning

confidence: 99%

Antimicrobial Peptides from Plants

et al. 2015

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“…Tam et al developed a selective bi-directional peptide bond cleavage approach utilizing N -methylcysteine (MeCys) in the Xaa-MeCys-Yaa peptides (Xaa and Yaa, non-cysteine residues) [ 146 ]. Under strong acidic conditions, peptide Xaa-MeCys-Yaa led to the formation of an oxazolinium intermediate, resulting in the cleavage of the Xaa-MeCys bond.…”

Section: Organic Molecules For Activation Of Amide Bondsmentioning

confidence: 99%

Amide Bond Activation of Biological Molecules

2018

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Amide bonds are the most prevalent structures found in organic molecules and various biomolecules such as peptides, proteins, DNA, and RNA. The unique feature of amide bonds is their ability to form resonating structures, thus, they are highly stable and adopt particular three-dimensional structures, which, in turn, are responsible for their functions. The main focus of this review article is to report the methodologies for the activation of the unactivated amide bonds present in biomolecules, which includes the enzymatic approach, metal complexes, and non-metal based methods. This article also discusses some of the applications of amide bond activation approaches in the sequencing of proteins and the synthesis of peptide acids, esters, amides, and thioesters.

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