A novel retro-inverso peptide is a preferential JNK substrate-competitive inhibitor

Ngoei, Kevin R.W.; Catimel, Bruno; Milech, Nadia; Watt, Paul M.; Bogoyevitch, Marie A.

doi:10.1016/j.biocel.2013.06.006

Cited by 8 publications

(9 citation statements)

References 73 publications

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“…The retroinverso version CADY-K peptide has been tried which has been successful in protecting it from proteolysis as well as retaining the capacity for cell penetration and self-assembly in form of nanoparticle with siRNA (Obasse, Taylor, Fullwood, & Allsop, 2017;Vaissière et al, 2017). The retroinverso analog of 18 residue long peptide PYC98 not only has fivefold more inhibition of the activity of JNK1 toward c-Jun but it also inhibits JNK1 activity toward EGFR-derived peptide (Ngoei, Catimel, Milech, Watt, & Bogoyevitch, 2013). The retroinverso analog of peptides have also been used for mimicking the carbohydrates for binding to an-nexin1 which has more selectivity than original peptide in targeting the tumor vasculature.…”

Section: Attempts Of Mimetics Using Retroinverso and Modified Analogsmentioning

confidence: 99%

“…Retroinverso melittin has fused to dioleoyl phosphoethanolamine for making a gene therapy vehicle riDOM, which has DNA binding as well as cell penetrating properties. Milletin has cell penetration properties whereas dioleoyl phosphoethanolamine binds DNA (Ngoei et al, 2013;Québatte, Kitas, & Seelig, 2013).…”

Section: And Simulation Studies On Retroinverso Peptidomimeticsmentioning

confidence: 99%

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Peptide and protein mimetics by retro and retroinverso analogs

Rai

2019

Chem Biol Drug Des

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Retroinverso analog of a natural polypeptide can sometimes mimic the structure and function of the natural peptide. The additional advantage of using retroinverso analog is that it is resistant to proteolysis. The retroinverso analogs have peptide sequence in reverse direction with respect to natural peptide and also have chirality of amino acid inverted from L to D. The D amino acids cannot be recognized by common proteases of the body; therefore, these peptides will not be degraded easily and have a longer‐lasting effect as vaccine and inhibitor drugs. There have been many contested propositions about the geometric relationship between a peptide and its retro, inverso, or retroinverso analog. A retroinverso analog sometimes fails to adopt the structure that can mimic the function of the natural peptide. In such cases, partial retroinverso analog and other modifications can help in achieving the desired structure and function. Here, we review the theory, major experimental attempts, prediction methods, and alternative strategies related to retroinverso peptidomimetics.

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Section: Attempts Of Mimetics Using Retroinverso and Modified Analogsmentioning

confidence: 99%

Section: And Simulation Studies On Retroinverso Peptidomimeticsmentioning

confidence: 99%

Peptide and protein mimetics by retro and retroinverso analogs

Rai

2019

Chem Biol Drug Des

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“…Finally, another method for stabilization consists in the substitution of L-amino acids with the corresponding D enantiomers. The synthesis of a retro-inverso (or inverted) peptide, D-amino acids assembled in the reverse order as compared to the parent L-sequence, leads to an analogue in which the side chains are usually arranged similarly to the native peptide [26] , [27] , [28] , [29] , [30] . Unfortunately, retro-inverted sequences not always maintain the bioactivity of the native peptide [31] , [32] .…”

Section: Introductionmentioning

confidence: 99%

Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides

Zamuner

Brun

Scorzeto

et al. 2017

Bioactive Materials

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Engineered scaffolds for bone tissue regeneration are designed to promote cell adhesion, growth, proliferation and differentiation. Recently, covalent and selective functionalization of glass and titanium surfaces with an adhesive peptide (HVP) mapped on [351–359] sequence of human Vitronectin allowed to selectively increase osteoblast attachment and adhesion strength in in vitro assays, and to promote osseointegration in in vivo studies. For the first time to our knowledge, in this study we investigated the resistance of adhesion sequences to proteolytic digestion: HVP was completely cleaved after 5 h. In order to overcome the enzymatic degradation of the native peptide under physiological conditions we synthetized three analogues of HVP sequence. A retro-inverted peptide D-2HVP, composed of D amino acids, was completely stable in serum-containing medium. In addition, glass surfaces functionalized with D-2HVP increased human osteoblast adhesion as compared to the native peptide and maintained deposition of calcium. Interestingly, D-2HVP increased expression of IBSP, VTN and SPP1 genes as compared to HVP functionalized surfaces. Total internal reflection fluorescence microscope analysis showed cells with numerous filopodia spread on D-2HVP-functionalized surfaces. Therefore, the D-2HVP sequence is proposed as new osteoblast adhesive peptide with increased bioactivity and high proteolytic resistance.

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“…58-60,[136][137][138][139][140][141] More recently, Ngoei et al identified the peptides L-PYC71N and D-PYC98 from a yeast twohybrid screen of a biodiverse gene fragment library 142,143. Both peptides are pan-JNK inhibitors…”

mentioning

confidence: 96%

Inhibitors of c-Jun N-Terminal Kinases: An Update

2014

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The c-Jun N-terminal kinases (JNKs) are serine/threonine kinases implicated in the pathogenesis of various diseases. Recent advances in the development of novel inhibitors of JNKs will be reviewed. Significant progress in the design of JNK inhibitors displaying selectivity versus other kinases has been achieved within the past 4 years. However, the development of isoform selective JNK inhibitors is still an open task.

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A novel retro-inverso peptide is a preferential JNK substrate-competitive inhibitor

Cited by 8 publications

References 73 publications

Peptide and protein mimetics by retro and retroinverso analogs

Peptide and protein mimetics by retro and retroinverso analogs

Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides

Inhibitors of c-Jun N-Terminal Kinases: An Update

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