Table 5 Functional implications and expected algorithmic suitability of gut-derived peptides based on their DISO study.

From: A comparative study of computational modeling approaches for evaluating structural dynamics and algorithmic suitability of short length peptides

AMP

Functional implications of disordered regions

Reason behind functional implications

Expected algorithmic suitability

Reason behind algorithmic suitability

Amp164

Versatile, adaptable antimicrobial action.

Fully disordered, coil-dominant structure allows flexible interaction with microbial targets47.

PEP-FOLD or AlphaFold

Fully disordered yet solvent-accessible regions favor PEP-FOLD36; AlphaFold balances moderate structure43.

Amp186

Effective balance of stability and flexibility.

Mixed structural fractions and solvent accessibility regions support stable but adaptable interactions47.

Modeller or AlphaFold

Stability from structural fractions and partial buried regions aligns with Modeller and AlphaFold’s capabilities43,45.

Amp218

Extreme flexibility for rapid, transient action.

Fully disordered and solvent-exposed regions enable transient interactions with membranes47.

PEP-FOLD (high disorder)

High disorder aligns well with PEP-FOLD’s ability36.

Amp2410

Rigid and strong membrane disruption capability.

Highly helical and solvent-exposed profile suggests strong, rigid interactions with microbial membranes2.

AlphaFold (rigid models)

Helical, rigid conformations are ideal for AlphaFold’s structured prediction capabilities35,43.

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