Oligo-peptoid Sequencing
Oligo-peptoid Sequencing - Related Videos
11:44
Synthesis and Mass Spectrometry Analysis of Oligo-peptoids
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Cited by 6 •
2018
A protocol is described for the manual synthesis of oligo-peptoids followed by sequence analysis by mass spectrometry.
09:34
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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2020
A protocol is presented for the synthesis of information-encoded peptoid oligomers and for the sequence-directed self-assembly of these peptoids into molecular ladders using amines and aldehydes as dynamic covalent reactant pairs and Lewis acidic rare-earth metal triflates as multi-role reagents.
12:02
An Efficient Method for the Synthesis of Peptoids with Mixed Lysine-type/Arginine-type Monomers and Evaluation of Their Anti-leishmanial Activity
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Cited by 8 •
2016
A protocol to synthesize peptoids with mixed cationic functionality in the same sequence is presented (lysine- and arginine-type monomers). Subsequent testing of these compounds against Leishmania mexicana, the protozoan parasites that cause cutaneous leishmaniasis, is also described.
08:43
OLIgo Mass Profiling (OLIMP) of Extracellular Polysaccharides
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Cited by 35 •
2010
A rapid way is described to gain insights into the structure of polysaccharides in an extracellular matrix. The method takes advantage of the specificity of glycosylhydrolases and the sensitivity of mass spectrometry allowing minute amounts of materials to be analyzed. This technique is adaptable to be used directly on tissue itself.
13:42
Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
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Cited by 40 •
2011
A simple and general manual peptoid synthesis method involving basic equipment and commercially available reagents is outlined, enabling peptoids to be easily synthesized in most laboratories. The synthesis, purification and characterization of an amphiphilic peptoid 36mer is described, as well as its self-assembly into highly-ordered nanosheets.
FAQs
Backbone fragmentation creates smaller peptoid-derived ions whose masses can be compared with the intact ion and with one another. The resulting mass differences correspond to incorporated side-chain units, allowing the analysis to reconstruct the order of monomers along the oligomer. This fragmentation-based approach connects measured ion masses to the molecular sequence rather than only to overall composition.
Diagnostic fragment ions provide sequence evidence that individual mass differences may not establish by themselves. Their identities and positions help assign particular side chains to specific locations within the oligomer, strengthening interpretation of the tandem mass spectrum. This is especially useful when confirming whether a synthesized product contains the intended arrangement of monomers.
Tandem mass spectrometry can distinguish the intended sequence from products containing deletions or substitutions. Fragmentation exposes changes in the monomer pattern, while mass differences and diagnostic ions indicate where the altered units occur. Consequently, the analysis can evaluate more than molecular presence: it can assess sequence fidelity and reveal specific deviations introduced during synthesis.
A typical workflow begins with ionizing the short peptoid so it can be analyzed as a mass-selected species. Tandem mass spectrometry then fragments the ion through its backbone, and the resulting fragment masses are examined for informative differences and diagnostic ions. Interpreting those signals yields the monomer identities and their positions for sequence verification.
Deletion and substitution products produce fragment patterns that differ from the expected sequence. Comparing observed mass differences and diagnostic fragment ions with the intended monomer arrangement can reveal a missing unit or an exchanged side chain. This makes the method useful for identifying synthesis byproducts and assessing whether a prepared peptoid matches its designed sequence.
Sequencing helps characterize peptoid libraries by linking each measured molecular composition to a defined monomer order. That information supports quality assessment across collections of related oligomers and clarifies which structures are being evaluated. In chemistry research, the resulting sequence assignments are relevant to sequence-defined materials, molecular recognition studies, antimicrobial candidates, and other peptoid-based functional molecules.