Final answer:
Hydrophobic amino acids are most likely to interact with lipids, especially within the lipid bilayer, where they engage in hydrophobic interactions with lipid tails, whereas amphipathic amino acids may interact at the interface of lipid head groups and the aqueous environment.
Step-by-step explanation:
Peptide-Lipid Interactions
When considering the interaction between peptides and lipids, hydrophobic amino acids are more likely to be involved in binding with the lipid portion of the membrane due to hydrophobic interactions. Proteins that are embedded in a lipid bilayer typically have amino acids with hydrophobic side chains in contact with the lipid tails, and amphipathic amino acids at the interface with the lipid head groups.
For example, a peptide sequence rich in leucine, isoleucine, valine, or phenylalanine would be expected to interact with the hydrophobic core of a lipid bilayer.
On the surface of a soluble protein, one would find hydrophilic amino acids, while the interior typically contains hydrophobic amino acids. This allows the protein to interact with the aqueous environment while maintaining structural integrity. In a protein embedded in a lipid bilayer, the exterior regions in contact with the lipid tails would be hydrophobic, while regions interacting with the aqueous environment would be hydrophilic.