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Paper-scoped peptide mentionSequence reported

MP

PMC9065177::PEP000001

Source publication

Polymer chimera of stapled oncolytic peptide coupled with anti-PD-L1 peptide boosts immunotherapy of colorectal cancer.

Theranostics · 2022

DOI 10.7150/thno.71129PMC9065177PMID 35547769
Sequence status
reported
Standardization
Sequence ready
Source location
text
Activity records
2

Sequence evidence

Reported molecular identity

INLKALAALAKKIL

The antimicrobial peptide mastoparan (MP, INLKALAALAKKIL), isolated from the venom of the wasp Vespula lewisii, is an α-helix peptide with 14 amino acid residues.

Resolved peptide links

PEPDIA-PLP-003679CTPDB_P081761

Experimental observations

Records linked to this mention

AnticancerCytotoxicPositive observation
Record detail

These stapled peptides were evaluated for cytotoxicity in the CRC cell line CT26 in vitro, IC50 values ranged from 1.11 μM to 9.32 μM. These stapled MP derivatives exhibited either enhanced or same anti-CRC activity, in comparison to the parent MP.

Mention PMC9065177::PEP000001PMC9065177text
Measure
other
Value
IC50 values ranged from 1.11 μM to 9.32 μM for stapled peptides; MP IC50 not explicitly given but stated stapled derivatives exhibited enhanced or same anti-CRC activity compared to parent MP
Target
CT26
Assay
Not reported by source
Source publication
ToxicityHemolyticPositive observation
Record detail

The potential of the stapled MP peptides to non-specifically lyse red blood cells (RBC) was measured and their hemolytic activities (HC50) determined. The peptide MP9 displayed the lowest level of RBC hemolysis.

Mention PMC9065177::PEP000001PMC9065177text
Measure
HD50
Value
HC50 values not explicitly given for MP; MP9 displayed the lowest level of RBC hemolysis
Target
Mus musculus
Assay
Not reported by source
Source publication

Local peptide labels such as P1, PEP1, or peptide 1 are grouped only within this paper and are not assumed to represent the same molecule across publications.