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Table 1 Types of AMPs based on structure

From: The dual interaction of antimicrobial peptides on bacteria and cancer cells; mechanism of action and therapeutic strategies of nanostructures

Category

Peptides

Sequence feature

Source

References

α Helical peptides

Aurein 1-2

Mellitin

Brevinin 1

Maculatins

Citropin

Buforin II

Cathelicidins:

-LL-37

-BMAP27,28,34

-Magainins

Cecropins

Amidated C-terminus

Amidated C-terminus

Amidated C-terminus

Amidated C-terminus

Amidated C-terminus

Amidated C-terminus

Frogs

Bees

Frogs

Frogs

Frogs

Toad

Humans

Bovine

Frogs

Insect

[29]

[30]

[31]

[32]

[33]

[34]

[35]

β-sheet peptides

Cathelicidins:

-Protegrins

-Bactenecin

Defensins:

-α-defensins

-β-defensins

-θ-defensins

Tachyplesins

Polyphemusin

Cysteine rich

Disulfide forming loop/arginine rich

Three disulfide bonds

Three disulfide bonds

Three disulfide bonds

Cysteine/arginine rich

Amidated C-terminus

Pigs

Bovine

Mammals

Mammals

Gorilla

Horse crab

Horse crab

[35]

[36]

[37]

[38]

Extended/

flexible

Cathelicidins:

-PR-39

-Tritrpticin

-Indolicidin

-Crotalicidin

Histatines

Proline and arginine rich

Tryptophan and arginine rich

Tryptophan and amidated C-terminus

Lysine rich

Histidine rich and amidated C-terminus

Pigs

Pigs

Bovine

Snakes

Humans

[35]

[39]

[40]