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Plant defensins are a prominent family of cationic peptides in the plant kingdom. They are structurally and functionally related to defensins that have been previously characterized in mammals and insects. They present molecular masses between 5 and 7kDa and possess a pattern of eight conserved Cys residues. The three-dimensional structure of plant defensins is small and globular. It has three anti-parallel beta-sheets and one alpha-helix that is stabilized by a structural motif composed of disulfide bridges. This motif is found in other peptides with biological activity and is called the Cys stabilized alphabeta motif (CSalphabeta). Based on the growing knowledge on defensin structure, gene expression and regulation, and also their in vitro biological activity, it has become clear that plant defensins are complex and sophisticated peptides whose function extends beyond their role in defense of plants against microbial infection. This review discusses recent data and will present comprehensive information regarding the study of defensins.

Plant lipid transfer proteins (LTP) are cationic peptides, subdivided into two families, which present molecular masses of around 7 and 10 kDa. The peptides were, thus, denominated due to their ability to reversibly bind and transport hydrophobic molecules in vitro. Both subfamilies possess conserved patterns of eight cysteine residues and the three-dimensional structure reveals an internal hydrophobic cavity that comprises the lipid binding site. Based on the growing knowledge regarding structure, gene expression and regulation and in vitro activity, LTPs are likely to play a role in key processes of plant physiology. Although the roles of plant LTPs have not yet been fully determined. This review aims to present comprehensive information of recent topics, cover new additional data, and present new perspectives on these families of peptides.