advantages of low-cost fabrication, disposability, and biocompatibility. [10] In particular, proteins have electrochemical properties, and therefore show promise in bioelectronic applications. Several groups have used proteins as the insulating layer in ReRAM. [7,[11][12][13] Albumen has recently been evaluated as a candidate for next-generation nonvolatile memory devices. [14,15] It has the advantages that it can be obtained directly from egg without extraction or further processing. Also, albumen has been applied as an insulating layer or dielectric layer to fabricate RS memory devices and thinfilm transistors. [9,16] Fe ions in the albumen form trap sites for electron transfer. If sufficient electrical bias is applied, reduced Fe ions form a conductive filament, so the albumen assumes LRS; then if sufficient opposite bias is applied, the Fe ions are oxidized, and the conductive filament ruptures, so the albumen assumes HRS. The presence of this RS effect suggests that albumen may be usable as an active layer in RS memory. Additionally, further improvement of the device's memory characteristics, such as reduced set voltage V SET and reset voltage V RESET or uniform switching properties, has been achieved by using ferritin protein to embed Pt nanoparticles (NPs) in NiO structure. [17] Also, embedding Au NPs in a silk protein layer reduced the V SET and V RESET of a ReRAM device. [18] In this study, we mixed Au NPs with albumen to improve its RS behavior. The charge-trapping characteristics of Au NPs were expected to reduce V SET and V RESET and give wide memory windows. [19] The use of protein-nanoparticle (P-NP) suspensions as memory has the disadvantage that the proteins interact and agglomerate with Au NPs in the solution, so the RS property in the fabricated memory devices changes. Therefore, controlling the degree of agglomeration is a key requirement to control the RS behaviors of ReRAM devices based on albumen with Au NPs. Proteins of albumen consist of amino chains that include sulfhydryl groups (R-SH), which can react with Au NPs and cause agglomeration; as a result, the memory characteristic changes from programmable RS to read-only memory. [11,20,21] Here, we characterize the RS behaviors of ReRAM based on albumen with Au NPs. We report how proteins interact with Au NPs to form clusters and affect the RS. We also suggest a switching mechanism of Au NPs-embedded protein-based ReRAM. This work is a significant step toward fabrication of biocompatible ReRAMs for configurable memory devices by controlling agglomeration of metal NPs in protein.Protein-nanoparticle (P-NP) interactions are of great importance in the biomedical applications, and are extensively studied for biotechnology and biomedicine applications, for example, cancer therapy, drug delivery, as well as biosafety area. Here, it is shown that P-NP interactions can have applications as resistive memory. It is demonstrated that the nature of resistive switching changes from programmable memory to read-only memory when the NPs aggregate in the pr...