Source 1primary paper2019ChemBioChem
Toolkit/de novo tripeptides containing glycine, tyrosine, and lysine
de novo tripeptides containing glycine, tyrosine, and lysine
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
De novo tripeptides composed of glycine, tyrosine, and lysine were reported to generate cyan fluorescence in vitro. The same study further indicates that amino acid identity and residue order modulate the fluorescent output, and that these peptides form robust dimer structures under moderate oxidizing conditions.
Usefulness & Problems
Why this is useful
These tripeptides are useful as a minimal peptide-based fluorescent system for studying how very short sequences can encode optical output. The reported sensitivity of fluorescence to residue identity and sequence also makes them a compact model for probing sequence–function relationships in de novo peptides.
Source:
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
Problem solved
This work addresses the problem of generating cyan fluorescence from an extremely small, de novo peptide scaffold rather than a larger canonical fluorescent protein. It also helps dissect how single-residue composition and sequence order influence fluorescence in such minimal systems.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
The reported observations were made in vitro, and dimer formation was observed under moderate oxidizing conditions. Beyond the peptide composition of glycine, tyrosine, and lysine, the supplied evidence does not specify construct formats, delivery methods, expression systems, or cofactor requirements.
The available evidence is limited to a single in vitro study and does not provide quantitative performance metrics such as excitation/emission maxima, brightness, quantum yield, or photostability. No evidence is provided here for cellular validation, in vivo function, or generalizability beyond the tested tripeptide variants.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
Approval Evidence
1 source3 linked approval claimsfirst-pass slug de-novo-tripeptides-containing-glycine-tyrosine-and-lysine
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
Source:
functional propertysupports
De novo tripeptides containing glycine, tyrosine, and lysine can generate cyan fluorescence.
Herein, we report an innovative approach to obtain cyan fluorescence by using de novo tripeptides containing glycine, tyrosine, and lysine
Source:
sequence function relationshipsupports
Both amino acid identity and sequence play significant roles in modulating fluorescence in the studied tripeptides.
Through an in vitro mutation approach, we deduce that both the amino acids and their sequence play significant roles in modulating the fluorescence.
Source:
structural propertysupports
The de novo tripeptides containing glycine, tyrosine, and lysine form robust dimer structures under moderate oxidizing conditions.
de novo tripeptides containing glycine, tyrosine, and lysine, which form robust dimer structures under moderate oxidizing conditions
Source:
Comparisons
Source-backed strengths
The reported tool is notable for achieving cyan fluorescence with only three amino acids: glycine, tyrosine, and lysine. The source study also reports that fluorescence is tunable by amino acid identity and sequence, and that the peptides form robust dimers under moderate oxidizing conditions.
Ranked Citations
- 1.